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  • 51.
    Bergsaker, H.
    et al.
    EUROfus Consortium, JET, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England.;KTH Royal Inst Technol, Sch Elect Engn, Dept Fus Plasma Phys, SE-10405 Stockholm, Sweden..
    Bykov, I.
    EUROfus Consortium, JET, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England.;KTH Royal Inst Technol, Sch Elect Engn, Dept Fus Plasma Phys, SE-10405 Stockholm, Sweden..
    Zhou, Y.
    EUROfus Consortium, JET, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England.;KTH Royal Inst Technol, Sch Elect Engn, Dept Fus Plasma Phys, SE-10405 Stockholm, Sweden..
    Petersson, P.
    EUROfus Consortium, JET, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England.;KTH Royal Inst Technol, Sch Elect Engn, Dept Fus Plasma Phys, SE-10405 Stockholm, Sweden..
    Possnert, Göran
    Uppsala University, Disciplinary Domain of Science and Technology, För teknisk-naturvetenskapliga fakulteten gemensamma enheter, Tandem Laboratory. EUROfus Consortium, JET, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England..
    Likonen, J.
    EUROfus Consortium, JET, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England.;VTT Tech Res Ctr Finland, POB 1000, FI-02044 Espoo, Finland..
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. EUROfus Consortium, JET, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England..
    Koivuranta, S.
    EUROfus Consortium, JET, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England.;VTT Tech Res Ctr Finland, POB 1000, FI-02044 Espoo, Finland..
    Widdowson, A. M.
    EUROfus Consortium, JET, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England.;CCFE, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England..
    Deep deuterium retention and Be/W mixing at tungsten coated surfaces in the JET divertor2016In: Physica Scripta, ISSN 0031-8949, E-ISSN 1402-4896, Vol. T167, article id 014061Article in journal (Refereed)
    Abstract [en]

    Surface samples from a full poloidal set of divertor tiles exposed in JET through operations 2010-2012 with ITER-like wall have been investigated using SEM, SIMS, ICP-AES analysis and micro beam nuclear reaction analysis (mu-NRA). Deposition of Be and retention of D is microscopically inhomogeneous. With careful overlaying of mu-NRA elemental maps with SEM images, it is possible to separate surface roughness effects from depth profiles at microscopically flat surface regions, without pits. With (He-3, p) mu-NRA at 3-5 MeV beam energy the accessible depth for D analysis in W is about 9 mu m, sufficient to access the W/Mo and Mo/W interfaces in the coatings and beyond, while for Be in W it is about 6 mu m. In these conditions, at all plasma wetted surfaces, D was found throughout the whole accessible depth at concentrations in the range 0.2-0.7 at% in W. Deuterium was found to be preferentially trapped at the W/Mo and Mo/W interfaces. Comparison is made with SIMS profiling, which also shows significant D trapping at the W/Mo interface. Mixing of Be and W occurs mainly in deposited layers.

  • 52.
    Bergström, L. Magnus
    et al.
    Department of Chemistry, Surface, and Corrosion Science, School of Chemical Science and Engineering, KTH Royal Institute of Technology, SE-10044 Stockholm, Sweden.
    Skoglund, Sara
    Department of Chemistry, Surface, and Corrosion Science, School of Chemical Science and Engineering, KTH Royal Institute of Technology, SE-10044 Stockholm, Sweden.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Eriksson, Jonny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Grillo, Isabelle
    Institut Laue Langevin, DS/LSS, 6 rue Jules Horowitz, BP156, 38042 Grenoble Cedex 9, France.
    Self-Assembly in Mixtures of an Anionic and a Cationic Surfactant: A Comparison between Small-Angle Neutron Scattering and Cryo-Transmission Electron Microscopy2013In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 29, no 38, p. 11834-11848Article in journal (Refereed)
    Abstract [en]

    The self-assembly in SOS-rich mixtures of the anionic surfactant sodium octyl sulfate (SOS) and the cationic surfactant hexadecyltrimethylammonium bromide (CTAB) has been investigated with the complementary techniques small-angle neutron scattering (SANS) and cryo-transmission electron microscopy (cryo-TEM). Both techniques confirm the simultaneous presence of open and closed bilayer structures in highly diluted samples as well as the existence of small globular and large elongated micelles at higher concentrations. However, the two techniques sometimes differ with respect to which type of aggregates is present in a particular sample. In particular, globular or wormlike micelles are sometimes observed with cryo-TEM in the vicinity of the micelle-to-bilayer transition, although only bilayers are present according to SANS and the samples appear bluish to the eye. A similar discrepancy has previously been reported but could not be satisfactorily rationalized. On the basis of our comparison between in situ (SANS) and ex situ (cryo-TEM) experimental techniques, we suggest that this discrepancy appears mainly as a result of the non-negligible amount of surfactant adsorbed at interfaces of the thin sample film created during the cryo-TEM specimen preparation. Moreover, from our detailed SANS data analysis, we are able to observe the unusually high amount of free surfactant monomers present in SOS-rich mixtures of SOS and CTAB, and the experimental results give excellent agreement with model calculations based on the Poisson?Boltzmann mean field theory. Our careful comparison between model calculations and experiments has enabled us to rationalize the dramatic microstructural transformations frequently observed upon simply diluting mixtures of an anionic and a cationic surfactant.

  • 53.
    Bergström, L. Magnus
    et al.
    School of Chemical Science and Engineering, Department of Chemistry, Surface and Corrosion Science, KTH Royal Institute of Technology, Sweden.
    Skoglund, Sara
    School of Chemical Science and Engineering, Department of Chemistry, Surface and Corrosion Science, KTH Royal Institute of Technology, Sweden.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Eriksson, Jonny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Grillo, Isabelle
    Institut Laue Langevin, DS/LSS, 6 rue Jules Horowitz, B.P. 156, 38042 Grenoble Cedex 9, France.
    Spontaneous Transformations between Surfactant Bilayers of Different Topologies Observed in Mixtures of Sodium Octyl Sulfate and Hexadecyltrimethylammonium Bromide2014In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 30, no 14, p. 3928-3938Article in journal (Refereed)
    Abstract [en]

    The influence of adding salt on the self-assembly in sodium octyl sulfate (SOS)-rich mixtures of the anionic surfactant SOS and the cationic surfactant hexadecyltrimethylammonium bromide (CTAB) have been investigated with the two complementary techniques, small-angle neutron scattering (SANS) and cryo-transmission electron microscopy. We are able to conclude that addition of a substantial amount of inert salt, NaBr, mainly has three effects on the structural behaviors: (i) the micelles become much larger at the transition from micelles to bilayers, (ii) the fraction of bilayer disks increases at the expense of vesicles, and (iii) bilayer aggregates perforated with holes are formed in the most diluted samples. A novel form factor valid for perforated bilayer vesicles and disks is introduced for the first time and, as a result, we are able to directly observe the presence of perforated bilayers by means of fitting SANS data with an appropriate model. Moreover, we are able to conclude that the morphology of bilayer aggregates changes according to the following sequence of different bilayer topologies, vesicles ? disks ? perforated bilayers, as the electrolyte concentration is increased and surfactant mole fraction in the bilayer aggregates approaches equimolarity. We are able to rationalize this sequence of transitions as a result of a monotonous increase of the bilayer saddle-splay constant (k?cbi) with decreasing influence from electrostatics, in agreement with theoretical predictions as deduced from the Poisson?Boltzmann theory.

  • 54.
    Bergström Lind, Sara
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Genomics. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Artemenko, Konstantin A
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Elfineh, Lioudmila
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Genomics. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Zhao, Yanhong
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Pettersson, Ulf
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Genomics. Uppsala University, Science for Life Laboratory, SciLifeLab.
    The phosphoproteome of the adenovirus type 2 virion2012In: Virology, ISSN 0042-6822, E-ISSN 1096-0341, Vol. 433, no 1, p. 253-261Article in journal (Refereed)
    Abstract [en]

    We have used a proteomics approach to identify sites of phosphorylation in the structural proteins of the Adenovirus type 2 particle. This protein modification might play an important role during infection. Peptides from highly purified virus were enriched for phosphorylations and analyzed by liquid chromatography-high-resolving mass spectrometry. Phosphorylations were identified in 11 structural peptides and 29 non-redundant phosphorylation sites were unambiguously assigned to specific amino acid. An unexpected result was the finding of phosphotyrosine in two of the viral polypeptides. The most highly phosphorylated protein was pIIIa with 12 identified phosphorylation sites. An identified preference for proline or leucine residue flanking the phosphorylation sites downstream suggests that cellular kinases are involved in many of the phosphorylations. Structural modeling showed that one site in the hexon is located on the outer side of the virus and could be of importance for the virus when attaching and entering cells.

  • 55.
    Bergström Lind, Sara
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Genomics.
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Pettersson, Ulf
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Genomics.
    A strategy for identification of protein tyrosine phosphorylation2012In: Methods, ISSN 1046-2023, E-ISSN 1095-9130, Vol. 56, no 2, p. 275-283Article in journal (Refereed)
    Abstract [en]

    To develop methods for studying phosphorylation of protein tyrosine residues is an important task since this protein modification regulates many cellular functions and often is involved in oncogenesis. An optimal protocol includes enrichment of tyrosine phosphorylated (pTyr) peptides or proteins, followed by a high resolving analytical method for identification of the enriched components. In this Methods paper, we describe a working strategy on how immunoaffinity enrichments, using anti-pTyr antibodies, combined with mass spectrometric (MS) analysis can be used to study the pTyr proteome. We describe in detail how our procedure was used to characterize the pTyr proteome of K562 leukemia cells. Important questions concerning the use of different anti-pTyr antibodies, enrichments performed at the peptide and/or the protein level, pooling of enrichments and requirements for the MS characterization are discussed.

  • 56. Bergvall, Ulrika A.
    et al.
    Co, Michelle
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Bergstrom, Roger
    Sjöberg, Per J. R.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Waldebäck, Monica
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Turner, Charlotta
    Anti-browsing effects of birch bark extract on fallow deer2013In: European Journal of Forest Research, ISSN 1612-4669, E-ISSN 1612-4677, Vol. 132, no 5-6, p. 717-725Article in journal (Refereed)
    Abstract [en]

    A major problem within forest industry is unwanted browsing on seedlings from mammalian herbivores. The aim of this study was to evaluate the effects of birch bark extracts as repellents towards fallow deer. Birch bark was extracted in a conventional way with ethanol as solvent at ambient temperature and with a new method, liquid CO2 extraction. An analysis of the ethanol-extracted birch bark showed that it contained large amounts of terpenoids, of which the most abundant was betulin. In seven different treatment trials, we used 15 individually handled fallow deer. To investigate the binary taste preferences, birch bark extract was added to food and presented in two bowls in typical two-choice tests. We found that the amount of a food type consumed during a trial and the number of shifts between food bowls were dependent on the amount of the birch extract the food contained. Concentrations of above 1 % by dry weight of birch extract acted as a repellent. In addition, such concentrations produced shorter feeding bouts by a greater willingness to change bowls. Therefore, our conclusion is that birch bark extract acts as a repellent towards fallow deer and is therefore likely to act as a repellent against other deer species. In addition, we show that birch bark extract produced by the new and more environmentally sustainable method employing liquid CO2 mixed with ethanol has the same repellent effect as the traditional ethanol extraction.

  • 57.
    Berndtson, Emma
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Qualitative analysis of LGD-4033 and its metabolites in equine plasma using UHPLC-MS(MS) for doping control purposes2017Independent thesis Advanced level (professional degree), 20 credits / 30 HE creditsStudent thesis
    Abstract [en]

    A new class of drugs has been developed for treatment of muscle and bone mass wasting diseases called non-steroidal selective androgen receptor modulators (SARMs). Because of their positive androgenic effects such as muscle gain, they are desirable as performance enhancers.

    One of those substances is LGD-4033 (4-[(2R)-2-[(1R)-2,2,2-trifluoro-1-hydroxyethyl]pyrrolidin-1-yl]-2-(trifluoromethyl)- benzonitrile). It has been detected in human samples in routine doping control and another SARM has been detected in an equine blood sample in routine doping control. It is therefore indicated that SARMs need to be screened for in routine testing in equestrian sport.

    The aim of this project was to identify what metabolites were found in equine plasma after an intra venous administration of LGD-4033 using UHPLC coupled with QToF-MS and determine whether the parent compound or any of its metabolites were most suitable for doping control.

    With the sample preparation method protein precipitation, six possible metabolites were identified in samples from three horses. Two of the metabolites were identified as phase I-metabolites (monohydroxylated and dihydroxylated). Four of the metabolites were identified as phase II-metabolites, where glucuronidation had occurred.

    The most suitable species for doping control were determined based on a semi- quantification and were M1a, M2 and M3a. 

  • 58.
    Berrier, Audrey
    et al.
    Universität Stuttgart, Physikalisches Institut, Germany.
    Schaafsma, Martijn C.
    FOM Institute AMOLF, Centre for Nanophotonics, c/o Philips Research Laboratories, Eindhoven, Netherlands.
    Nonglaton, Guillaume
    CEA Leti, MINATEC Campus, Department of microtechnologies for Biology and Healthcare, France.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Rivas, Jaime Gómez
    FOM Institute AMOLF, Centre for Nanophotonics, c/o Philips Research Laboratories AND COBRA Research Institute, Eindhoven University of Technology, Netherlands .
    Selective detection of bacterial layers with terahertz plasmonic antennas2012In: Biomedical Optics Express, ISSN 2156-7085, E-ISSN 2156-7085, Vol. 3, no 11, p. 2937-2949Article in journal (Refereed)
    Abstract [en]

    Current detection and identification of micro-organisms is based on either rather unspecific rapid microscopy or on more accurate complex, time-consuming procedures. In a medical context, the determination of the bacteria Gram type is of significant interest. The diagnostic of microbial infection often requires the identification of the microbiological agent responsible for the infection, or at least the identification of its family (Gram type), in a matter of minutes. In this work, we propose to use terahertz frequency range antennas for the enhanced selective detection of bacteria types. Several microorganisms are investigated by terahertz time-domain spectroscopy: a fast, contactless and damage-free investigation method to gain information on the presence and the nature of the microorganisms. We demonstrate that plasmonic antennas enhance the detection sensitivity for bacterial layers and allow the selective recognition of the Gram type of the bacteria.

  • 59.
    Bertilsson, Sarah
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Glycanmapping of glycoproteins with UPLC-FLR-MALDI/TOF-MS2014Independent thesis Advanced level (degree of Master (Two Years)), 20 credits / 30 HE creditsStudent thesis
  • 60.
    Bivehed, Erik
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Strömvall, Robert
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bakalkin, Georgy
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Andersson, Malin
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Region-specific bioconversion of dynorphin neuropeptide detected by in situ histochemistry and MALDI imaging mass spectrometry2017In: Peptides, ISSN 0196-9781, E-ISSN 1873-5169, Vol. 87, p. 20-27Article in journal (Refereed)
    Abstract [en]

    Brain region-specific expression of proteolytic enzymes can control the biological activity of endogenous neuropeptides and has recently been targeted for the development of novel drugs, for neuropathic pain, cancer, and Parkinson's disease. Rapid and sensitive analytical methods to profile modulators of enzymatic activity are important for finding effective inhibitors with high therapeutic value. Combination of in situ enzyme histochemistry with MALDI imaging mass spectrometry allowed developing a highly sensitive method for analysis of brain-area specific neuropeptide conversion of synthetic and endogenous neuropeptides, and for selection of peptidase inhibitors that differentially target conversion enzymes at specific anatomical sites. Conversion and degradation products of Dynorphin B as model neuropeptide and effects of peptidase inhibitors applied to native brain tissue sections were analyzed at different brain locations. Synthetic dynorphin B (2 pmol) was found to be converted to the N-terminal fragments on brain sections whereas fewer C-terminal fragments were detected. N-ethylmaleimide (NEM), a non-selective inhibitor of cysteine peptidases, almost completely blocked the conversion of dynorphin B to dynorphin B(1-6; Leu-Enk-Arg), (1-9), (2-13), and (7-13). Proteinase inhibitor cocktail, and also incubation with acetic acid displayed similar results. Bioconversion of synthetic dynorphin B was region-specific producing dynorphin B(1-7) in the cortex and dynorphin B (2-13) in the striatum. Enzyme inhibitors showed region-and enzyme-specific inhibition of dynorphin bioconversion. Both phosphoramidon (inhibitor of the known dynorphin converting enzyme neprilysin) and opiorphin (inhibitor of neprilysin and aminopeptidase N) blocked cortical bioconversion to dynorphin B(1-7), wheras only opiorphin blocked striatal bioconversion to dynorphin B(2-13). This method may impact the development of novel therapies with aim to strengthen the effects of endogenous neuropeptides under pathological conditions such as chronic pain. Combining histochemistry and MALDI imaging MS is a powerful and sensitive tool for the study of inhibition of enzyme activity directly in native tissue sections. (C) 2016 The Authors. Published by Elsevier Inc.

  • 61.
    Blom, Magnus
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Synthetical Organic Chemistry.
    Norrehed, Sara
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Synthetical Organic Chemistry.
    Andersson, Claes-Henrik
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Synthetical Organic Chemistry.
    Huang, Hao
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Nanotechnology and Functional Materials.
    Light, Mark E.
    Department of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, U.K.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Grennberg, Helena
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Physical Organic Chemistry.
    Gogoll, Adolf
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Synthetical Organic Chemistry.
    Synthesis and Properties of Bis-Porphyrin Molecular Tweezers: Effects of Spacer Flexibility on Binding and Supramolecular Chirogenesis2016In: Molecules, ISSN 1420-3049, E-ISSN 1420-3049, Vol. 21, no 1Article in journal (Refereed)
    Abstract [en]

    Abstract: Ditopic binding of various dinitrogen compounds to three bisporphyrin molecular tweezers with spacers of varying conformational rigidity, incorporating the planar ene-diyne (1), the helical stiff stilbene (2), or the semirigid glycoluril motif fused to  the porphyrins (3) are compared. Binding constants Ka = 10^4 to 10^6 M^-1 reveal subtle  differences between these tweezers, that are discussed in terms of porphyrin dislocation  modes. Exciton coupled circular dichroism (ECCD) of complexes with chiral dinitrogen  guests provides experimental evidence for the conformational properties of the tweezers. The results are further supported and rationalized by conformational analysis.

  • 62.
    Bodvik, Rasmus
    et al.
    KTH Royal Institute of Technology, School of Chemical Science and Engineering, Department of Chemistry, Surface and Corrosion Science, Sweden.
    Karlson, Lief
    Akzo Nobel Functional Chemicals AB, Sweden.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Eriksson, Jonny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Thormann, Esben
    KTH Royal Institute of Technology, School of Chemical Science and Engineering, Department of Chemistry, Surface and Corrosion Science, Sweden.
    Claesson, Per Martin
    FRIAS, School of Soft Matter Research, University of Freiburg, Germany AND KTH Royal Institute of Technology, School of Chemical Science and Engineering, Department of Chemistry, Surface and Corrosion Science, Sweden.
    Aggregation of modified celluloses in aqueous solution: transition from methylcellulose to hydroxypropylmethylcellulose solution properties induced by a low molecular weight oxyethylene additive2012In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 28, no 38, p. 13562-13569Article in journal (Refereed)
    Abstract [en]

    Temperature effects on viscosity and aggregation behaviour of aqueous solutions of three different cellulose ethers: methylcellulose (MC), hydroxypropylmethylcellulose (HPMC) and ethyl(hydroxyethyl)cellulose (EHEC), were investigated using viscosity and dynamic light scattering measurements as well as Cryo-TEM. In all cases increasing temperature reduces the solvent quality of water, which induces aggregation. It was found that the aggregation rate followed the order EHEC > HPMC > MC, suggesting that cellulose ethers containing some bulky and partly hydrophilic substituents assemble into large aggregates more readly than methylcellulose. This finding is discussed in terms of the organization of the structures formed by the different cellulose ethers. The temperature-dependent association behavior of cellulose ethers was also investigated in a novel way by adding diethyleneglycolmonobutylether (BDG) to methylcellulose aqueous solutions. When the concentration of BDG was at and above 5 wt%, methylcellulose adopted HPMC-like solution behaviour. In particular, a transition temperature where the viscosity was decreasing, prior to increasing at higher temperatures, appeared and the aggregation rate increased. This observation is rationalized by the ability of the amphiphilic BDG to accumulate at non-polar interfaces, and thus also to associate with hydrophobic regions of methylcellulose. In effect BDG is suggested to act as a physisorbed hydrophilic and bulky substituent inducing similar constraints on aggregation as the chemically attached hydroxypropyl groups in HPMC and oligo(ethyleneoxide) chains in EHEC.

  • 63. Boge, Lucas
    et al.
    Bysell, Helena
    Ringstad, Lovisa
    Wennman, David
    Umerska, Anita
    Cassisa, Viviane
    Eriksson, Jonny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Joly-Guillou, Marie-Laure
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Andersson, Martin
    Lipid-Based Liquid Crystals As Carriers for Antimicrobial Peptides: Phase Behavior and Antimicrobial Effect2016In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 32, no 17, p. 4217-4228Article in journal (Refereed)
    Abstract [en]

    The number of antibiotic-resistant bacteria is increasing worldwide, and the demand for novel antimicrobials is constantly growing. Antimicrobial peptides (AMPs) could be an important part of future treatment strategies of various bacterial infection diseases. However, AMPs have relatively low stability, because of proteolytic and chemical degradation. As a consequence, carrier systems protecting the AMPs are greatly needed, to achieve efficient treatments. In addition, the carrier system also must administrate the peptide in a controlled manner to match the therapeutic dose window. In this work, lyotropic liquid crystalline (LC) structures consisting of cubic glycerol monooleate/water and hexagonal glycerol monooleate/oleic acid/water have been examined as carriers for AMPs. These LC structures have the capability of solubilizing both hydrophilic and hydrophobic substances, as well as being biocompatible and biodegradable. Both bulk gels and discrete dispersed structures (i.e., cubosomes and hexosomes) have been studied. Three AMPs have been investigated with respect to phase stability of the LC structures and antimicrobial effect: AP114, DPK-060, and LL-37. Characterization of the LC structures was performed using small-angle X-ray scattering (SAXS), dynamic light scattering, zeta-potential, and cryogenic transmission electron microscopy (Cryo-TEM) and peptide loading efficacy by ultra performance liquid chromatography. The antimicrobial effect of the LCNPs was investigated in vitro using minimum inhibitory concentration (MIC) and time-kill assay. The most hydrophobic peptide (AP114) was shown to induce an increase in negative curvature of the cubic LC system. The most polar peptide (DPK-060) induced a decrease in negative curvature while LL-37 did not change the LC phase at all. The hexagonal LC phase was not affected by any of the AMPs. Moreover, cubosomes loaded with peptides AP114 and DPK-060 showed preserved antimicrobial activity, whereas particles loaded with peptide LL-37 displayed a loss in its broad-spectrum bactericidal properties. AMP-loaded hexosomes showed a reduction in antimicrobial activity.

  • 64. Boge, Lukas
    et al.
    Umerska, Anita
    Matougui, Nada
    Bysell, Helena
    Ringstad, Lovisa
    Davoudi, Mina
    Eriksson, Jonny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Andersson, Martin
    Cubosomes post-loaded with antimicrobial peptides: characterization, bactericidal effect and proteolytic stability.2017In: International Journal of Pharmaceutics, ISSN 0378-5173, E-ISSN 1873-3476, Vol. 526, no 1-2, p. 400-412Article in journal (Refereed)
    Abstract [en]

    Novel antibiotics, such as antimicrobial peptides (AMPs), have recently attended more and more attraction. In this work, dispersed cubic liquid crystalline gel (cubosomes) was used as drug delivery vehicles for three AMPs (AP114, DPK-060 and LL-37). Association of peptides onto cubosomes was studied at two cubosome/peptide ratios using high performance liquid chromatography, ζ-potential and circular dichroism measurements. AMPs impact on the cubosome structure was investigated using small angle x-ray scattering and cryogenic transmission electron microscopy. The antimicrobial effect of the AMP loaded cubosomes was studied in vitro by minimum inhibitory concentration and time-kill assays. Proteolytic protection was investigated by incubating the formulations with two elastases and the antimicrobial effect after proteolysis was studied using radial diffusion assay. Different association efficacy onto the cubosomes was observed among the AMPs, with LL-37 showing greatest association (>60%). AP114 loaded cubosomes displayed a preserved antimicrobial effect, whereas for LL-37 the broad spectrum bacterial killing was reduced to only comprise Gram-negative bacteria. Interestingly, DPK-060 loaded cubosomes showed a slight enhanced effect against S. aureus and E. coli strains. Moreover, the cubosomes were found to protect LL-37 from proteolytic degradation, resulting in a significantly better bactericidal effect after being subjected to elastase, compared to unformulated peptide.

  • 65.
    Boge, Lukas
    et al.
    RISE Res Inst Sweden, Div Biosci & Mat, Stockholm, Sweden; Chalmers Univ Technol, Chem & Chem Engn, Gothenburg, Sweden.
    Umerska, Anita
    MINT Univ Angers, Angers, France.
    Matougui, Nada
    MINT Univ Angers, Angers, France.
    Bysell, Helena
    RISE Res Inst Sweden, Div Biosci & Mat, Stockholm, Sweden.
    Ringstad, Lovisa
    RISE Res Inst Sweden, Div Biosci & Mat, Stockholm, Sweden.
    Davoudi, Mina
    Lund Univ, Dept Clin Sci, Lund, Sweden.
    Eriksson, Jonny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Andersson, Martin
    Chalmers Univ Technol, Chem & Chem Engn, Gothenburg, Sweden.
    Liquid crystalline particles for delivery of antimicrobial peptides2018In: Abstract of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 255Article in journal (Other academic)
  • 66. Boge, Lukas
    et al.
    Västberg, Amanda
    Umerska, Anita
    Bysell, Helena
    Eriksson, Jonny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Millqvist-Fureby, Anna
    Andersson, Martin
    Freeze-dried and re-hydrated liquid crystalline nanoparticles stabilized with disaccharides for drug-delivery of the plectasin derivative AP114 antimicrobial peptide2018In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 522, p. 126-135Article in journal (Refereed)
    Abstract [en]

    Liquid crystalline nanoparticles (LCNPs), e.g. cubosomes and hexosomes, are receiving more and more attraction as drug delivery vehicles. Dry powder formulation that forms LCNPs upon hydration can be advantageous to make new routes of administration accessible. In this work, we investigate use of three disaccharides (lactose, trehalose and sucrose) as protective matrices for glycerol monooleate based LCNP forming powders produced by freeze-drying. Phase behavior, particle size and size distributions at the different preparation steps were monitored by small angle x-ray scattering (SAXS) and dynamic light scattering (DLS). Particle appearance was imaged by cryogenic transmission electron microscopy (cryo-TEM). Moreover, the therapeutic relevant antimicrobial peptide AP114 (plectasin derivative) was incorporated in the formulations. Peptide encapsulation and release as well as in vitro antibacterial effect were investigated. Results showed that all freeze-dried powders did form particles with liquid crystalline structure upon hydration. However, a phase transition from the bicontinuous cubic Pn3m to the reversed hexagonal was observed, as a consequence of sugar addition and the freeze-drying procedure. Data indicates that trehalose is the preferred choice of lyo-protectant in order to maintain a mono-modal particle size distribution. In addition, antimicrobial activity of AP114-containing formulations was found to be highest for the formulation containing trehalose. The release kinetics of AP114 from the nanoparticles was strongly affected by the dimensions of the hexagonal phase. Larger dimension of the hexagonal phase, significantly improved the release of AP114 and antimicrobial activity of the formulation.

  • 67. Bonnet, Cecilia
    et al.
    Rusz, Jan
    Megrelishvili, Marika
    Sieger, Tomas
    Matouskova, Olga
    Okujava, Michael
    Brozova, Hana
    Nikolai, Tomas
    Hanuska, Jaromir
    Kapianidze, Mariam
    Mikeladze, Nina
    Botchorishvili, Nazi
    Khatiashvili, Irine
    Janelidze, Marina
    Serranova, Tereza
    Fiala, Ondrej
    Roth, Jan
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Jech, Robert
    Rivaud-Pechoux, Sophie
    Gaymard, Bertrand
    Ruzicka, Evzen
    Eye Movements in Ephedrone-Induced Parkinsonism2014In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 9, no 8, p. e104784-Article in journal (Refereed)
    Abstract [en]

    Patients with ephedrone parkinsonism (EP) show a complex, rapidly progressive, irreversible, and levodopa non-responsive parkinsonian and dystonic syndrome due to manganese intoxication. Eye movements may help to differentiate parkinsonian syndromes providing insights into which brain networks are affected in the underlying disease, but they have never been systematically studied in EP. Horizontal and vertical eye movements were recorded in 28 EP and compared to 21 Parkinson's disease (PD) patients, and 27 age- and gender-matched healthy subjects using standardized oculomotor tasks with infrared videooculography. EP patients showed slow and hypometric horizontal saccades, an increased occurrence of square wave jerks, long latencies of vertical antisaccades, a high error rate in the horizontal antisaccade task, and made more errors than controls when pro-and antisaccades were mixed. Based on oculomotor performance, a direct differentiation between EP and PD was possible only by the velocity of horizontal saccades. All remaining metrics were similar between both patient groups. EP patients present extensive oculomotor disturbances probably due to manganese-induced damage to the basal ganglia, reflecting their role in oculomotor system.

  • 68.
    Botling Taube, Amelie
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Konzer, Anne
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Alm, Albert
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Ophthalmology.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Proteomic Analysis of the Aqueous Humor in Eyes with Pseudoexfoliation SyndromeArticle in journal (Refereed)
  • 69.
    Botling Taube, Amelie
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience. Karolinska Inst, Dept Clin Neurosci, St Erik Eye Hosp, Stockholm, Sweden.
    Konzer, Anne
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Alm, Albert
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Proteomic analysis of the aqueous humour in eyes with pseudoexfoliation syndrome2019In: British Journal of Ophthalmology, ISSN 0007-1161, E-ISSN 1468-2079, Vol. 103, no 8, p. 1190-1194Article in journal (Refereed)
    Abstract [en]

    Background/aims Pseudoexfoliation syndrome (PEX) is characterised by the production and accumulation of extracellular fibrillar material in the anterior segment of the eye. The pathogenesis of PEX is multifactorial with genetic factors and ageing as contributing factors. Previously, an increased concentration of beta-crystalline B2 (CRYBB2) was observed in the aqueous humour (AH) in eyes with PEX in a pooled material. Here, the protein content was examined on individual basis. Methods During cataract surgery, AH was sampled from patients with and without PEX, 10 eyes in each group. The proteins were digested and labelled with isotopomeric dimethyl labels, separated with high-pressure liquid chromatography and analysed in an Orbitrap mass analyzer. Results The concentration of complement factor 3, kininogen-1, antithrombin III and vitamin D-binding protein was increased in all eyes with PEX. Retinol-binding protein 3, glutathione peroxidase, calsyntenin-1 and carboxypeptidase E were decreased in eyes with PEX. Beta-crystalline B1 and CRYBB2 and gamma-crystalline D were up to eightfold upregulated in 4 of 10 in eyes with PEX. Conclusion The results indicate that oxidative stress and inflammation are contributing factors in the formation of PEX. Knowledge about the proteome in PEX is relevant for understanding this condition.

  • 70.
    Botling Taube, Amelie
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Mi, Jia
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Alm, Albert
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Ophthalmology.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Imaging of Human Lens Capsules with Pseudoexfoliation Syndrome by Time of Flight Secondary Ion Mass Spectrometry (TOF-SIMS)Manuscript (preprint) (Other academic)
  • 71.
    Bowden, John A.
    et al.
    NIST, Marine Biochem Sci Grp, Div Chem Sci, Hollings Marine Lab, Charleston, SC 29412 USA..
    Heckert, Alan
    NIST, Stat Engn Div, Gaithersburg, MD 20899 USA..
    Ulmer, Candice Z.
    NIST, Marine Biochem Sci Grp, Div Chem Sci, Hollings Marine Lab, Charleston, SC 29412 USA..
    Jones, Christina M.
    NIST, Marine Biochem Sci Grp, Div Chem Sci, Hollings Marine Lab, Charleston, SC 29412 USA..
    Koelmel, Jeremy P.
    Univ Florida, Dept Pathol Immunol & Lab Med, Gainesville, FL USA..
    Abdullah, Laila
    Roskamp Inst, Sarasota, FL USA..
    Ahonen, Linda
    Steno Diabet Ctr Copenhagen, Gentofte, Denmark..
    Alnouti, Yazen
    Univ Nebraska, Med Ctr, Dept Pharmaceut Sci, Omaha, NE USA..
    Armando, Aaron M.
    Univ Calif San Diego, Sch Med, Dept Chem & Biochem, La Jolla, CA 92093 USA.;Univ Calif San Diego, Sch Med, Dept Pharmacol, La Jolla, CA 92093 USA..
    Asara, John M.
    Beth Israel Deaconess Med Ctr, Div Signal Transduct, Boston, MA 02215 USA.;Harvard Med Sch, Dept Med, Boston, MA USA..
    Bamba, Takeshi
    Kyushu Univ, Med Inst Bioregulat, Res Ctr Trans Med, Div Metabol,Higashi Ku, Fukuoka, Japan..
    Barr, John R.
    Natl Ctr Environm Hlth, Ctr Dis Control & Prevent, Div Lab Sci, Atlanta, GA USA..
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Borchers, Christoph H.
    Univ Victoria, Genome British Columbia Prote Ctr, Victoria, BC, Canada.;Univ Victoria, Dept Biochem & Microbiol, Victoria, BC, Canada.;McGill Univ, Jewish Gen Hosp, Gerald Bronfman Dept Oncol, Montreal, PQ, Canada.;McGill Univ, Jewish Gen Hosp, Prote Ctr, Segal Canc Ctr,Lady Davis Inst, Montreal, PQ, Canada..
    Brandsma, Joost
    Univ Southampton, Southampton Gen Hosp, Acad Unit Clin & Expt Sci, Fac Med, Southampton, Hants, England..
    Breitkopf, Susanne B.
    Beth Israel Deaconess Med Ctr, Div Signal Transduct, Boston, MA 02215 USA..
    Cajka, Tomas
    Univ Calif Davis, Genome Ctr, Natl Inst Hlth West Coast Metabol Ctr, Davis, CA 95616 USA..
    Cazenave-Gassiot, Amaury
    Natl Univ Singapore, Yong Loo Lin Sch Med, Dept Biochem, Singapore, Singapore.;Singapore Lipidomic Incubator SLING, Inst Life Sci, Singapore, Singapore..
    Checa, Antonio
    Karolinska Inst, Dept Med Biochem & Biophys, Div Physiol Chem 2, Stockholm, Sweden..
    Cinel, Michelle A.
    Baker Heart & Diabet Inst, Melbourne, Vic, Australia..
    Colas, Romain A.
    Brigham & Womens Hosp, Ctr Expt Therapeut & Reperfus Injury, Dept Anesthesiol Perioperat & Pain Med, 75 Francis St, Boston, MA 02115 USA.;Harvard Med Sch, Boston, MA USA..
    Cremers, Serge
    Columbia Univ, Med Ctr, Irving Inst Clin & Translat Res, Biomarker Core Lab, New York, NY USA..
    Dennis, Edward A.
    Univ Calif San Diego, Sch Med, Dept Chem & Biochem, La Jolla, CA 92093 USA.;Univ Calif San Diego, Sch Med, Dept Pharmacol, La Jolla, CA 92093 USA..
    Evans, James E.
    Roskamp Inst, Sarasota, FL USA..
    Fauland, Alexander
    Karolinska Inst, Dept Med Biochem & Biophys, Div Physiol Chem 2, Stockholm, Sweden..
    Fiehn, Oliver
    Univ Calif Davis, Genome Ctr, Natl Inst Hlth West Coast Metabol Ctr, Davis, CA 95616 USA.;King Abdulaziz Univ, Biochem Dept, Jeddah, Saudi Arabia..
    Gardner, Michael S.
    Natl Ctr Environm Hlth, Ctr Dis Control & Prevent, Div Lab Sci, Atlanta, GA USA..
    Garrett, Timothy J.
    Univ Florida, Dept Pathol Immunol & Lab Med, Gainesville, FL USA..
    Gotlinger, Katherine H.
    New York Med Coll, Sch Med, Dept Pharmacol, Valhalla, NY 10595 USA..
    Han, Jun
    Univ Victoria, Genome British Columbia Prote Ctr, Victoria, BC, Canada..
    Huang, Yingying
    Thermo Fisher Sci, San Jose, CA USA..
    Neo, Aveline Huipeng
    Natl Univ Singapore, Yong Loo Lin Sch Med, Dept Biochem, Singapore, Singapore.;Singapore Lipidomic Incubator SLING, Inst Life Sci, Singapore, Singapore..
    Hyotylainen, Tuulia
    Orebro Univ, Dept Chem, Orebro, Sweden..
    Izumi, Yoshihiro
    Kyushu Univ, Med Inst Bioregulat, Res Ctr Trans Med, Div Metabol,Higashi Ku, Fukuoka, Japan..
    Jiang, Hongfeng
    Columbia Univ, Med Ctr, Irving Inst Clin & Translat Res, Biomarker Core Lab, New York, NY USA..
    Jiang, Houli
    New York Med Coll, Sch Med, Dept Pharmacol, Valhalla, NY 10595 USA..
    Jiang, Jiang
    Univ Calif San Diego, Sch Med, Dept Chem & Biochem, La Jolla, CA 92093 USA.;Univ Calif San Diego, Sch Med, Dept Pharmacol, La Jolla, CA 92093 USA..
    Kachman, Maureen
    Univ Michigan, BRCF, Metabol Core, Ann Arbor, MI 48109 USA..
    Kiyonami, Reiko
    Thermo Fisher Sci, San Jose, CA USA..
    Klavins, Kristaps
    Biocrates Life Sci AG, Innsbruck, Austria..
    Klose, Christian
    Lipotype GmbH, Dresden, Germany..
    Kofeler, Harald C.
    Med Univ Graz, Core Facil Mass Spectrometry, Graz, Austria..
    Kolmert, Johan
    Karolinska Inst, Dept Med Biochem & Biophys, Div Physiol Chem 2, Stockholm, Sweden..
    Koal, Therese
    Biocrates Life Sci AG, Innsbruck, Austria..
    Koster, Grielof
    Univ Southampton, Southampton Gen Hosp, Acad Unit Clin & Expt Sci, Fac Med, Southampton, Hants, England..
    Kuklenyik, Zsuzsanna
    Natl Ctr Environm Hlth, Ctr Dis Control & Prevent, Div Lab Sci, Atlanta, GA USA..
    Kurland, Irwin J.
    Albert Einstein Coll Med, Diabet Res Ctr, Stable Isotope & Metabol Core Facil, Bronx, NY 10467 USA..
    Leadley, Michael
    Hosp Sick Children, Res Inst, Analyt Facil Bioact Mol, Toronto, ON, Canada..
    Lin, Karen
    Univ Victoria, Genome British Columbia Prote Ctr, Victoria, BC, Canada..
    Maddipati, Krishna Rao
    Wayne State Univ, Lipid Core Facil, Detroit, MI USA.;Wayne State Univ, Dept Pathol, Detroit, MI USA..
    McDougall, Danielle
    Univ Florida, Dept Pathol Immunol & Lab Med, Gainesville, FL USA..
    Meikle, Peter J.
    Baker Heart & Diabet Inst, Melbourne, Vic, Australia..
    Mellett, Natalie A.
    Baker Heart & Diabet Inst, Melbourne, Vic, Australia..
    Monnin, Cian
    Concordia Univ, Dept Chem & Biochem, Montreal, PQ, Canada..
    Moseley, M. Arthur
    Duke Univ, Sch Med, Levine Sci Res Ctr, Prote & Metabol Shared Resource, Durham, NC USA..
    Nandakumar, Renu
    Columbia Univ, Med Ctr, Irving Inst Clin & Translat Res, Biomarker Core Lab, New York, NY USA.;Lipotype GmbH, Dresden, Germany..
    Oresic, Matej
    Univ Turku, Turku Ctr Biotechnol, Turku, Finland.;Abo Akad Univ, Turku, Finland..
    Patterson, Rainey
    Peake, David
    Pierce, Jason S.
    Post, Martin
    Hosp Sick Children, Res Inst, Analyt Facil Bioact Mol, Toronto, ON, Canada..
    Postle, Anthony D.
    Pugh, Rebecca
    NIST, Chem Sci Div, Environm Specimen Bank Grp, Hollings Marine Lab, Charleston, SC USA..
    Qiu, Yunping
    Albert Einstein Coll Med, Diabet Res Ctr, Stable Isotope & Metabol Core Facil, Bronx, NY 10467 USA..
    Quehenberger, Oswald
    Univ Calif San Diego, Sch Med, Dept Med, La Jolla, CA 92093 USA.;Univ Calif San Diego, Sch Med, Dept Pharmacol, La Jolla, CA 92093 USA..
    Ramrup, Parsram
    Rees, Jon
    Natl Ctr Environm Hlth, Ctr Dis Control & Prevent, Div Lab Sci, Atlanta, GA USA..
    Rembiesa, Barbara
    Med Univ South Carolina, Dept Biochem & Mol Biol, Charleston, SC USA..
    Reynaud, Denis
    Hosp Sick Children, Res Inst, Analyt Facil Bioact Mol, Toronto, ON, Canada..
    Roth, Mary R.
    Kansas State Univ, Kansas Lipid Res Ctr, Div Biol, Manhattan, KS 66506 USA..
    Sales, Susanne
    Max Planck Inst Mol Cell Biol & Genet, Dresden, Germany..
    Schuhmann, Kai
    Max Planck Inst Mol Cell Biol & Genet, Dresden, Germany..
    Schwartzman, Michal Laniado
    New York Med Coll, Sch Med, Dept Pharmacol, Valhalla, NY 10595 USA..
    Serhan, Charles N.
    Brigham & Womens Hosp, Ctr Expt Therapeut & Reperfus Injury, Dept Anesthesiol Perioperat & Pain Med, 75 Francis St, Boston, MA 02115 USA.;Harvard Med Sch, Boston, MA USA..
    Shevchenko, Andrej
    Max Planck Inst Mol Cell Biol & Genet, Dresden, Germany..
    Somerville, Stephen E.
    Med Univ South Carolina, Hollings Marine Lab, Charleston, SC USA..
    John-Williams, Lisa St.
    Duke Univ, Sch Med, Levine Sci Res Ctr, Prote & Metabol Shared Resource, Durham, NC USA..
    Surma, Michal A.
    Univ Michigan, BRCF, Metabol Core, Ann Arbor, MI 48109 USA..
    Takeda, Hiroaki
    Kyushu Univ, Med Inst Bioregulat, Res Ctr Trans Med, Div Metabol,Higashi Ku, Fukuoka, Japan..
    Thakare, Rhishikesh
    Univ Nebraska, Med Ctr, Dept Pharmaceut Sci, Omaha, NE USA..
    Thompson, J. Will
    Duke Univ, Sch Med, Levine Sci Res Ctr, Prote & Metabol Shared Resource, Durham, NC USA..
    Torta, Federico
    Natl Univ Singapore, Yong Loo Lin Sch Med, Dept Biochem, Singapore, Singapore.;Singapore Lipidomic Incubator SLING, Inst Life Sci, Singapore, Singapore..
    Triebl, Alexander
    Med Univ Graz, Core Facil Mass Spectrometry, Graz, Austria..
    Troetzmueller, Martin
    Med Univ Graz, Core Facil Mass Spectrometry, Graz, Austria..
    Ubhayasekera, S. J. Kumari
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Vuckovic, Dajana
    Weir, Jacquelyn M.
    Baker Heart & Diabet Inst, Melbourne, Vic, Australia..
    Welti, Ruth
    Kansas State Univ, Kansas Lipid Res Ctr, Div Biol, Manhattan, KS 66506 USA..
    Wenk, Markus R.
    Natl Univ Singapore, Yong Loo Lin Sch Med, Dept Biochem, Singapore, Singapore.;Singapore Lipidomic Incubator SLING, Inst Life Sci, Singapore, Singapore..
    Wheelock, Craig E.
    Karolinska Inst, Dept Med Biochem & Biophys, Div Physiol Chem 2, Stockholm, Sweden..
    Yao, Libin
    Kansas State Univ, Kansas Lipid Res Ctr, Div Biol, Manhattan, KS 66506 USA..
    Yuan, Min
    Beth Israel Deaconess Med Ctr, Div Signal Transduct, Boston, MA 02215 USA..
    Zhao, Xueqing Heather
    Albert Einstein Coll Med, Diabet Res Ctr, Stable Isotope & Metabol Core Facil, Bronx, NY 10467 USA..
    Zhou, Senlin
    Wayne State Univ, Lipid Core Facil, Detroit, MI USA.;Wayne State Univ, Dept Pathol, Detroit, MI USA..
    Harmonizing lipidomics: NIST interlaboratory comparison exercise for lipidomics using SRM 1950-Metabolites in Frozen Human Plasma2017In: Journal of Lipid Research, ISSN 0022-2275, E-ISSN 1539-7262, Vol. 58, no 12, p. 2275-2288Article in journal (Refereed)
    Abstract [en]

    As the lipidomics field continues to advance, self-evaluation within the community is critical. Here, we performed an interlaboratory comparison exercise for lipidomics using Standard Reference Material (SRM) 1950-Metabolites in Frozen Human Plasma, a commercially available reference material. The interlaboratory study comprised 31 diverse laboratories, with each laboratory using a different lipidomics workflow. A total of 1,527 unique lipids were measured across all laboratories and consensus location estimates and associated uncertainties were determined for 339 of these lipids measured at the sum composition level by five or more participating laboratories. These evaluated lipids detected in SRM 1950 serve as community-wide benchmarks for intra-and interlaboratory quality control and method validation. These analyses were performed using nonstandardized laboratory-independent workflows. The consensus locations were also compared with a previous examination of SRM 1950 by the LIPID MAPS consortium.jlr While the central theme of the interlaboratory study was to provide values to help harmonize lipids, lipid mediators, and precursor measurements across the community, it was also initiated to stimulate a discussion regarding areas in need of improvement.

  • 72. Bozaykut, Perinur
    et al.
    Sozen, Erdi
    Kaga, Elif
    Ece, Asli
    Ozaltin, Esra
    Ek, Bo
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Ozer, Nesrin Kartal
    Grune, Tilman
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Karademir, Betul
    The role of heat stress on the age related protein carbonylation2013In: Journal of Proteomics, ISSN 1874-3919, E-ISSN 1876-7737, Vol. 89, p. 238-254Article in journal (Refereed)
    Abstract [en]

    Since the proteins are involved in many physiological processes in the organisms, modifications of proteins have important outcomes. Protein modifications are classified in several ways and oxidative stress related ones take a wide place. Aging is characterized by the accumulation of oxidized proteins and decreased degradation of these proteins. On the other hand protein turnover is an important regulatory mechanism for the control of protein homeostasis. Heat shock proteins are a highly conserved family of proteins in the various cells and organisms whose expressions are highly inducible during stress conditions. These proteins participate in protein assembly, trafficking, degradation and therefore play important role in protein turnover. Although the entire functions of each heat shock protein are still not completely investigated, these proteins have been implicated in the processes of protection and repair of stress-induced protein damage. This study has focused on the heat stress related carbonylated proteins, as a marker of oxidative protein modification, in young and senescent fibroblasts. The results are discussed with reference to potential involvement of induced heat shock proteins. This article is part of a Special Issue entitled: Protein Modifications. Biological significance Age-related protein modifications, especially protein carbonylation take a wide place in the literature. In this direction, to highlight the role of heat shock proteins in the oxidative modifications may bring a new aspect to the literature. On the other hand, identified carbonylated proteins in this study confirm the importance of folding process in the mitochondria which will be further analyzed in detail.

  • 73.
    Brishammar, Sture
    et al.
    MASE Laboratory, Uppsala, Sweden.
    Hanrieder, Jörg
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    TMV-particle borne enhancer of a tobacco RNA-replicase2012In: World Journal of Science and Technology, ISSN 2231-2587, Vol. 2, no 7, p. 4-7Article in journal (Refereed)
    Abstract [en]

    According to separation studies it has been evident that a tobacco RNA-replicase after TMV-infection consists of two parts. The larger part is host-directed and will be combined with a virus borne small protein which considerably enhances the RNA-replicase activity and is therefore named replicase enhancer, Ree. This compound was found at HPLC-separations of TMV-coat proteins, and was detected using polymerase assay with a radioactive nucleotide involved. Molecular weight has been determined by mass spectrometry: with FT ICR MS to get the size – 6 023.3 - and with MALDI TOF MS to obtain a sequence of the 54 amino acids involved. Presumably Ree is fixed to the TMV-RNA at infection. The enzyme seems to produce minus-strands of the virus RNA.

  • 74.
    Bunrit, Anon
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Dahlstrand, Christian
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Olsson, Sandra K.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Srifa, Pemikar
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Huang, Genping
    Orthaber, Andreas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
    Sjöberg, Per J. R.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Biswas, Srijit
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Himo, Fahmi
    Samec, Joseph S. M.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Bronsted Acid-Catalyzed Intramolecular Nucleophilic Substitution of the Hydroxyl Group in Stereogenic Alcohols with Chirality Transfer2015In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 137, no 14, p. 4646-4649Article in journal (Refereed)
    Abstract [en]

    The hydroxyl group of enantioenriched benzyl, propargyl, allyl, and alkyl alcohols has been intramolecularly displaced by uncharged O-, N-, and S-centered nucleophiles to yield enantioenriched tetrahydrofuran, pyrrolidine, and tetrahydrothiophene derivatives with phosphinic acid catalysis. The five-membered heterocyclic products are generated in good to excellent yields, with high degree of chirality transfer, and water as the only side-product. Racemization experiments show that phosphinic acid does not promote S(N)1 reactivity. Density functional theory calculations corroborate a reaction pathway where the phosphinic acid operates as a bifunctional catalyst in the intramolecular substitution reaction. In this mechanism, the acidic proton of the phosphinic acid protonates the hydroxyl group, enhancing the leaving group ability. Simultaneously, the oxo group of phosphinic acid operates as a base abstracting the nucleophilic proton and thus enhancing the nucleophilicity. This reaction will open up new atom efficient techniques that enable alcohols to be used as nucleofuges in substitution reactions in the future.

  • 75.
    Bunrit, Anon
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC. Stockholm Univ, Dept Organ Chem, S-10691 Stockholm, Sweden..
    Sawadjoon, Supaporn
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Tsupova, Svetlana
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Sjöberg, Per J. R.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Samec, Joseph S. M.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC. Stockholm Univ, Dept Organ Chem, S-10691 Stockholm, Sweden..
    A General Route to beta-Substituted Pyrroles by Transition-Metal Catalysis2016In: Journal of Organic Chemistry, ISSN 0022-3263, E-ISSN 1520-6904, Vol. 81, no 4, p. 1450-1460Article in journal (Refereed)
    Abstract [en]

    An atom-efficient route to pyrroles substituted in the beta-position has been achieved in four high yielding steps by a combination of Pd, Ru, and Fe catalysis with only water and ethene as side-products. The reaction is general and gives pyrroles substituted in the beta-position with linear and branched alkyl, benzyl, or aryl groups in overall good yields. The synthetic route includes a Pd-catalyzed monoallylation step of amines with substituted allylic alcohols that proceeds to yield the monoallylated products in moderate to excellent yields. In a second step, unsymmetrical diallylated aromatic amines are generated from the reaction of a second allylic alcohol with high selectivity in moderate to good yields by control of the reaction temperature. Ru-catalyzed ring-closing metathesis performed on the diallylated aromatic amines yields the pyrrolines substituted in the beta-position in excellent yields. By addition of ferric chloride to the reaction mixture, a selective aromatization to yield the corresponding pyrroles substituted in the beta-position was achieved. A reaction mechanism involving a palladium hydride, generated from insertion of palladium to O-H of an allyl alcohol, that is responsible for the C-O bond cleavage to generate the pi-allyl intermediate is proposed.

  • 76.
    Bykov, I.
    et al.
    Royal Inst Technol KTH, Div Fus Plasma Phys, Stockholm, Sweden..
    Bergsåker, H.
    Royal Inst Technol KTH, Div Fus Plasma Phys, Stockholm, Sweden..
    Possnert, Göran
    Uppsala University, Disciplinary Domain of Science and Technology, För teknisk-naturvetenskapliga fakulteten gemensamma enheter, Tandem Laboratory.
    Zhou, Y.
    Royal Inst Technol KTH, Div Fus Plasma Phys, Stockholm, Sweden..
    Heinola, K.
    Univ Helsinki, Dept Phys, POB 64, Helsinki 00560, Finland..
    Pettersson, Jean
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Conroy, Sean
    Uppsala University, Disciplinary Domain of Science and Technology, Physics, Department of Physics and Astronomy, Applied Nuclear Physics.
    Likonen, J.
    VTT, POB 1000, Espoo 02044, Finland..
    Petersson, P.
    Royal Inst Technol KTH, Div Fus Plasma Phys, Stockholm, Sweden..
    Widdowson, A.
    EUROfus Consortium, JET, Culham Sci Ctr, Abingdon OX14 3DB, Oxon, England..
    Studies of Be migration in the JET tokamak using AMS with Be-10 marker2016Conference paper (Refereed)
    Abstract [en]

    The JET tokamak is operated with beryllium limiter tiles in the main chamber and tungsten coated carbon fiber composite tiles and solid W tiles in the divertor. One important issue is how wall materials are migrating during plasma operation. To study beryllium redistribution in the main chamber and in the divertor, a Be-10 enriched limiter tile was installed prior to plasma operations in 2011-2012. Methods to take surface samples have been developed, an abrasive method for bulk Be tiles in the main chamber, which permits reuse of the tiles, and leaching with hot HCl to remove all Be deposited at W coated surfaces in the divertor. Quantitative analysis of the total amount of Be in cm(2) sized samples was made with inductively coupled plasma atomic emission spectroscopy (ICP-AES). The Be-10/Be-9 ratio in the samples was measured with accelerator mass spectrometry (AMS). The experimental setup and methods are described in detail, including sample preparation, measures to eliminate contributions in AMS from the B-10 isobar, possible activation due to plasma generated neutrons and effects of diffusive isotope mixing. For the first time marker concentrations are measured in the divertor deposits. They are in the range 0.4-1.2% of the source concentration, with moderate poloidal variation.

  • 77.
    Cadu, Alban
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Synthetical Organic Chemistry.
    Watile, Rahul
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Biswas, Srijit
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Orthaber, Andreas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström.
    Sjöberg, Per J
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Samec, Joseph
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Synthetical Organic Chemistry.
    One-Pot Synthesis of Keto Thioethers by Palladium/Gold-Catalyzed Click and Pinacol Reactions2014In: Organic Letters, ISSN 1523-7060, E-ISSN 1523-7052, Vol. 16, no 21, p. 5556-5559Article in journal (Refereed)
    Abstract [en]

    An atom-efficient synthesis of keto thioethers was devised via tandem gold/palladium catalysis. The reaction proceeds through a regioselective thiol attack at the β-position of the alcohol, followed by an alkyl, aryl, or benzyl 1,2-shift. Both acyclic and cyclic systems were studied, in the latter case leading to the ring expansion of cyclic substrates.

  • 78.
    Cardoso-Palacios, Carlos
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Lanekoff, Ingela
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Direct Analysis of Pharmaceutical Drugs Using Nano-DESI MS2016In: Journal of Analytical Methods in Chemistry, ISSN 2090-8865, E-ISSN 2090-8873, article id 3591908Article in journal (Refereed)
    Abstract [en]

    Counterfeit pharmaceutical drugs imply an increasing threat to the global public health. It is necessary to have systems to control the products that reach the market and to detect falsified medicines. In this work, molecules in several pharmaceutical tablets were directly analyzed using nanospray desorption electrospray ionization mass spectrometry (nano-DESI MS). Nano-DESI is an ambient surface sampling technique which enables sampling of molecules directly from the surface of the tablets without any sample pretreatment. Both the active pharmaceutical ingredients (APIs) and some excipients were detected in all analyzed tablets. Principal component analysis was used to analyze mass spectral features from different tablets showing strong clustering between tablets with different APIs. The obtained results suggest nano-DESI MS as future tool for forensic analysis to discern APIs present in unknown tablet samples.

  • 79.
    Carlsson, Anna-Carin C
    et al.
    Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
    Grafenstein, Jurgen
    Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
    Budnjo, Adnan
    Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
    Laurila, Jesse L
    Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Karim, Alavi
    Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
    Kleinmaier, Roland
    Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
    Brath, Ulrika
    Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
    Erdelyi, Mate
    Department of Chemistry and Molecular Biology, University of Gothenburg and The Swedish NMR Centre, Gothenburg, Sweden.
    Symmetric halogen bonding is preferred in solution2012In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 134, no 12, p. 5706-5715Article in journal (Refereed)
    Abstract [en]

    Halogen bonding is a recently rediscovered secondary interaction that shows potential to become a complementary molecular tool to hydrogen bonding in rational drug design and in material sciences. Whereas hydrogen bond symmetry has been the subject of systematic studies for decades, the understanding of the analogous three-center halogen bonds is yet in its infancy. The isotopic perturbation of equilibrium (IPE) technique with 13C NMR detection was applied to regioselectively-deuterated pyridine complexes to investigate the symmetry of [N–I–N]+ and [N–Br–N]+ halogen bonding in solution. Preference for a symmetric arrangement was observed for both a freely adjustable and for a conformationally restricted [N–X–N]+ model system, as also confirmed by computation on the DFT level. A closely attached counter ion is shown to be compatible with the preferred symmetric arrangement. The experimental observations and computational predictions reveal a high energetic gain upon formation of symmetric, three-center four-electron halogen bonding. Whereas hydrogen bonds are generally asymmetric in solution and symmetric in the crystalline state, the analogous bromine and iodine centered halogen bonds prefer symmetric arrangement in solution.

  • 80.
    Carlsson, Anna-Carin C.
    et al.
    Department of Chemistry and the Swedish NMR Centre, University of Gothenburg, Sweden.
    Grafenstein, Jurgen
    Department of Chemistry and the Swedish NMR Centre, University of Gothenburg, Sweden.
    Laurila, Jesse L.
    Department of Chemistry and the Swedish NMR Centre, University of Gothenburg, Sweden.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Erdelyi, Mate
    Department of Chemistry and the Swedish NMR Centre, University of Gothenburg, Sweden.
    Symmetry of [N-X-N]+ halogen bonds in solution2012In: Chemical Communications, ISSN 1359-7345, E-ISSN 1364-548X, Vol. 48, no 10, p. 1458-1460Article in journal (Refereed)
    Abstract [en]

    The first investigation of halogen bond symmetry is presented. In contrast to related hydrogen bonds, the iodous halogen bond is symmetric in solution and in the crystal. The bromous analogue is symmetric in solution, but shows asymmetry in the solid state. NMR results are in agreement with DFT predictions.

  • 81.
    Carlsson, Jörgen
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Oncology, Radiology and Clinical Immunology, Biomedical Radiation Sciences.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Ghaneolhosseini, H
    Gedda, Lars
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Oncology, Radiology and Clinical Immunology, Biomedical Radiation Sciences.
    Johnsson, M
    Sjöberg, S
    Stabilised liposomes with double targeting intendent for use in BNCT2001In: Frontiers in Neutron Capture Therapy: Volume 1 / [ed] M Frederick Hawthorne, Kenneth Shelly, Richard J Wiersema, 2001, p. 184-Conference paper (Other academic)
  • 82.
    Carter, Sarah-Sophia
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Atif, Abdul
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Lanekoff, Ingela
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Tenje, Maria
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Mestres, Gemma
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Tailoring the biocompatibility of the elastomer PDMS for on-chip applications2018Conference paper (Refereed)
  • 83.
    Carter, Sarah-Sophia
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Atif, Abdul Raouf M.
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Lanekoff, Ingela
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Tenje, Maria
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Mestres, Gemma
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Improving the biocompatibility of PDMS by improving its curing time and temperature2018Conference paper (Other academic)
  • 84.
    Cedernaes, Jonathan
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Functional Pharmacology.
    Schonke, Milena
    Karolinska Inst, Dept Mol Med & Surg, Solna, Sweden.
    Westholm, Jakub Orzechowski
    Stockholm Univ, Dept Biochem & Biophys, Sci Life Lab, Stockholm, Sweden.
    Mi, Jia
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Binzhou Med Univ, Med & Pharmarcy Res Ctr, Yantai, Peoples R China.
    Chibalin, Alexander
    Karolinska Inst, Dept Mol Med & Surg, Solna, Sweden.
    Voisin, Sarah
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Functional Pharmacology.
    Osler, Megan
    Karolinska Inst, Dept Mol Med & Surg, Solna, Sweden.
    Vogel, Heike
    German Inst Human Nutr Potsdam Rehbrucke, Dept Expt Diabetol, Potsdam, Germany.
    Hornaeus, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Dickson, Suzanne L.
    Univ Gothenburg, Sahlgrenska Acad, Inst Neurosci & Physiol, Dept Physiol Endocrinol, Gothenburg, Sweden.
    Lind, Sara
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Univ Utah, Dept Pathol, Salt Lake City, UT 84132 USA;Binzhou Med Univ, Precis Med, Yantai, Peoples R China.
    Schiöth, Helgi B.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Functional Pharmacology.
    Zierath, Juleen R.
    Karolinska Inst, Dept Mol Med & Surg, Solna, Sweden.
    Benedict, Christian
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Functional Pharmacology.
    Acute sleep loss results in tissue-specific alterations in genome-wide DNA methylation state and metabolic fuel utilization in humans2018In: Science Advances, E-ISSN 2375-2548, Vol. 4, no 8, article id eaar8590Article in journal (Refereed)
    Abstract [en]

    Curtailed sleep promotes weight gain and loss of lean mass in humans, although the underlying molecular mechanisms are poorly understood. We investigated the genomic and physiological impact of acute sleep loss in peripheral tissues by obtaining adipose tissue and skeletal muscle after one night of sleep loss and after one full night of sleep. We find that acute sleep loss alters genome-wide DNA methylation in adipose tissue, and unbiased transcriptome-, protein-, and metabolite-level analyses also reveal highly tissue-specific changes that are partially reflected by altered metabolite levels in blood. We observe transcriptomic signatures of inflammation in both tissues following acute sleep loss, but changes involving the circadian clock are evident only in skeletal muscle, and we uncover molecular signatures suggestive of muscle breakdown that contrast with an anabolic adipose tissue signature. Our findings provide insight into how disruption of sleep and circadian rhythms may promote weight gain and sarcopenia.

  • 85.
    Chen, Moashan
    et al.
    LaTrobeUniversity.
    Hongxing, Zhao
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Medicinsk genetik och genomik.
    Bergström Lind, Sara
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Pettersson, Ulf
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Medicinsk genetik och genomik.
    Data on the expression of cellular lncRNAs in human adenovirus infected cells2016In: Data in Brief, E-ISSN 2352-3409, Vol. 8, p. 1263-1279Article in journal (Refereed)
    Abstract [en]

    Expression of cellular long non-coding RNAs (lncRNAs) in human primary lung fibroblasts (IMR-90) during the course of adenovirus type 2 (Ad2) infection was studied by strand-specific whole transcriptome sequencing. In total, 645 cellular lncRNAs were expressed at a significant level and 398 of them were changed more than 2-fold. The changes in expression followed a distinct temporal pattern. Significantly, 80% of the changes occurred at the late phase and 80% of the de-regulated lncRNAs were up-regulated. The three largest groups of deregulated lncRNAs were 125 antisense RNAs, 111 pseudogenes and 85 long intergenic non-coding RNAs (lincRNAs). Lastly, more than 36% of lncRNAs have been shown to interact with RNA binding proteins.

  • 86.
    Chowdhury, Azazul Islam
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Hörnaeus, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergsten, Peter
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology. Uppsala Univ, Med Cell Biol, Uppsala, Sweden..
    Role of PIAS1 in palmitate mediated beta cell dysfunction2015In: Diabetologia, ISSN 0012-186X, E-ISSN 1432-0428, Vol. 58, no Suppl. 1, p. S230-S230Article in journal (Other academic)
  • 87.
    Chowdhury, Azazul
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Satagopam, Venkata P.
    Manukyan, Levon
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Fung, Yi Man Eva
    Schneider, Reinhard
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Bergsten, Peter
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
    Signaling in Insulin-Secreting MIN6 Pseudoislets and Monolayer Cells2013In: Journal of Proteome Research, ISSN 1535-3893, E-ISSN 1535-3907, Vol. 12, no 12, p. 5954-5962Article in journal (Refereed)
    Abstract [en]

    Cell cell interactions are of fundamental importance for cellular function. In islets of Langerhans, which control blood glucose levels by secreting insulin in response to the blood . glucose concentration, the secretory response of intact islets is c higher than that of insulin-producing beta-cells not arranged in the islet architecture. The objective was to define mechanisms by which cellular performance is enhanced when cells are arranged in a) three-dimensional space. The task was addressed by making a c comprehensive analysis based on protein expression patterns " generated from insulin-secreting MIN6 cells grown as islet-like c clusters, so-called pseudoislets, and in monolayers. After culture, glucose-stimulated insulin secretion (GSIS) was measured from monolayers and pseudoislets. GSIS rose 6-fold in pseudoislets but only 3-fold in monolayers when the glucose concentration was increased from 2 to 20 mmol/L. Proteins from pseudoislets and monolayers were extracted and analyzed by liquid-chromatography mass spectrometry, and differentially expressed proteins were mapped onto KEGG pathways. Protein profiling identified 1576 proteins, which were common to pseudoislets and monolayers. When mapped onto KEGG pathways, 11 highly enriched pathways were identified. On the basis of differences in expression of proteins belonging to the pathways in pseudoislets and monolayers, predictions of differential pathway activation were performed. Mechanisms enhancing insulin secretory capacity of the beta-cell, when situated in the islet, include pathways regulating glucose metabolism, cell interaction, and translational regulation.

  • 88.
    Chu, Jiangtao
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Undin, Torgny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergström Lind, Sara
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Hjort, Klas
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Dahlin, Andreas
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Influence of surface modification and static pressure on microdialysis protein extraction efficiency2015In: Biomedical microdevices (Print), ISSN 1387-2176, E-ISSN 1572-8781, Vol. 17, no 5, article id UNSP 96Article in journal (Refereed)
    Abstract [en]

    There is growing interest in using microdialysis (MD) for monitoring larger and more complexmolecules such as neuropeptides and proteins. This promotes the use of MD membranes withmolecular weight cut off (MWCO) of 100 kDa or above. The hydrodynamic property of themembrane goes to ultrafiltration or beyond, making the MD catheters more sensitive to pressure.In the meantime, despite the large pore size, studies have shown that membrane biofouling stilllead to unstable catheter performance. The objective is to study in vitro how 500 kDa dextranand Poloxamer 407 surface modification affect the fluid recovery (FR) and extraction efficiency(EE) of 100 kDa MWCO MD catheters. A pressure chamber was designed to facilitate the tests,using as MD sample a protein standard with similar concentrations as in human cerebral spinalfluid, comparing native and Poloxamer 407 modified MD catheters. The collected dialysatefractions were examined for FR and protein EE, employing Dot-it Spot-it Protein Assay for totalprotein EE and targeted mass spectrometry (MS) for EE of individual proteins and peptides. TheFR results suggested that the surface modified catheters were less sensitive to the pressure andprovide higher precision, and provided a FR closer to 100%. The surface modification did notshow a significant effect on the protein EE. The average total protein EE of surface modifiedcatheters was slightly higher than that of the native ones. The MS EE data of individual proteinsshowed a clear trend of complex response in EE with pressure.

  • 89.
    Chu, Jiangtao
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Undin, Torgny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Dahlin, Andreas
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Wang, Cong
    Park, Jungyul
    Hjort, Klas
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Protein Desalination Chip for Mass Spectrometry Sample Preparation2015Conference paper (Refereed)
    Abstract [en]

    This work focuses on desalination of a protein sample in a lab-on-chip device using the ion concentration polarization (ICP) technique. It was demonstrated with a salt containing buffer with four proteins and two peptides of concentrations typical to cerebrospinal fluid (CSF). Not only was the output desalinated but its protein concentration with large molecular weight (MW) was as much as 3 times higher for the largest protein compared to the original. We conclude that ICP based microfluidic chips have great potential for desalination and protein concentration in microdialysis sampling coupled to mass spectroscopy (MS).

  • 90.
    Chu, Jiangtao
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Undin, Torgny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Lind, Sara
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Dahlin, Andreas
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Hjort, Klas
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Influence of different pluronic surface modifications and pressure on microdialysis protein extraction efficiency2015In: Biomedical microdevices (Print), ISSN 1387-2176, E-ISSN 1572-8781Article in journal (Refereed)
    Abstract [en]

    There is growing interest in using microdialysis (MD) for monitoring larger and more complexmolecules such as neuropeptides and proteins. This promotes the use of MD membranes withmolecular weight cut off (MWCO) of 100 kDa. Hence, the hydrodynamic property of themembrane goes to ultrafiltration, making the sampling more sensitive to pressure changes. Also,despite the large membrane pore size, studies have shown that membrane biofouling still leads tounstable catheter performance. Our objective is to study in vitro how four kinds of surfacemodifications (Pluronic L31, L44, F87 and F127+L31) affect the fluid recovery (FR) andextraction efficiency (EE) of 100 kDa MWCO MD catheters, under controlled pressure. Apressure chamber was employed to facilitate the tests, using as MD sample a protein standardwith proteins of similar concentrations as in human cerebral spinal fluid. The collected dialysatefractions were examined for FR and EE. Targeted mass spectrometry analysed the EE ofindividual proteins and peptides. The thicker the pluronic adsorption layer, the less thehydrodynamic diameter of the membrane pores, leading to lower and more stable FR. The foursurface modifications had three different behaviours: Pluronic F127 + L31 showed similarbehavior to the Pluronic F127 and the native original membrane; Pluronic F87 showed acontinuous EE increase with pressure; Pluronic L31 and L44 showed similar EE values, whichwere stable with pressure. Different surface modifications are clearly selective to differentproteins and peptides. We conclude that a pluronic surface modification could provide MDsampling with more stable FR, and more stable or enhanced EE with high FR, depending on theobjective of the sampling.

  • 91.
    Co, Michelle
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Zettersten, Camilia
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Nyholm, Leif
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Inorganic Chemistry.
    Sjöberg, Per J.R
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Turner, Charlotta
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Degradation effects in the extraction of antioxidants from birch bark using water at elevated temperature and pressure2012In: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 716, p. 40-48Article in journal (Refereed)
    Abstract [en]

    Experiments with birch bark samples have been carried to enable a distinction between extraction and degradation effects during pressurised hot water extraction. Two samples, E80 and El 80, contained birch bark extracts obtained after extraction at 80 and 180 degrees C for up to 45 min, respectively. Two other samples, P80 and P180, were only extracted for 5 min at the two temperatures and were thereafter filtered and hydrothermally treated at 80 and 180 degrees C, respectively. During the latter treatment, samples were collected at different times to assess the stability of the extracted compounds. An offline DPPH (2,2-diphenyl-1-picrylhydrazyl) assay, as well as a high performance liquid chromatographic separation coupled to an electrochemical detector, were used to determine the antioxidant capacity of the processed samples. The results obtained with the different techniques were compared to assess the yield of the extraction and degradation processes. In addition, an online hyphenated system comprising high performance liquid chromatography coupled to diode-array; electrochemical; and tandem mass spectrometric detection (HPLC-DAD-ECD-MS/MS) was used to study the compositions of the extracts in more detail. The results for the samples processed at 80 degrees C showed that the extraction reached a steady-state already after 5 min, and that the extracted compounds were stable throughout the entire extraction process. Processing at 180 degrees C, on the other hand, gave rise to partly degraded extracts with a multitude of peaks in both the diode array and electrochemical detectors, and a higher antioxidant capacity compared to for the extracts obtained at 80 degrees C. It is concluded that HPLC-DAD-ECD is a more appropriate technique for the determination of antioxidants than the DPPH assay. The mass spectrometric results indicate that one of the extracted antioxidants, catechin, was isomerised to its diastereoisomers; (+)-catechin, (-)-catechin, (+)-epicatechin, and (-)-epicatechin.

     

  • 92.
    Corpeno, Rebeca
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Dworkin, Barry
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Cacciani, Nicola
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Salah, Heba
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Bergman, Hilde-Marlene
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Ravara, B
    Vitadello, M
    Gorza, Luisa
    Gustafson, Ann-Marie
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Hedström, Yvette
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Petersson, J
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Feng, H-Z
    Jin, Jian-Ping
    Iwamoto, Hiroyuki
    Yagi, Naoto
    Artemenko, Konstantin
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Bergquist, Jonas
    Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Larsson, Lars
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Clinical Neurophysiology.
    Time-course analysis of mechanical ventilation-induced diaphragm contractile muscle dysfunction in the rat2014In: Journal of Physiology, ISSN 0022-3751, E-ISSN 1469-7793, Vol. 592, no 17, p. 3859-3880Article in journal (Refereed)
    Abstract [en]

    Controlled mechanical ventilation (CMV) plays a key role in triggering the impaired diaphragm muscle function and the concomitant delayed weaning from the respirator in critically ill intensive care unit (ICU) patients. To date, experimental and clinical studies have primarily focused on early effects on the diaphragm by CMV, or at specific time points. To improve our understanding of the mechanisms underlying the impaired diaphragm muscle function in response to mechanical ventilation, we have performed time‐resolved analyses between 6 h and 14 days using an experimental rat ICU model allowing detailed studies of the diaphragm in response to long‐term CMV. A rapid and early decline in maximum muscle fibre force and preceding muscle fibre atrophy was observed in the diaphragm in response to CMV, resulting in an 85% reduction in residual diaphragm fibre function after 9–14 days of CMV. A modest loss of contractile proteins was observed and linked to an early activation of the ubiquitin proteasome pathway, myosin:actin ratios were not affected and the transcriptional regulation of myosin isoforms did not show any dramatic changes during the observation period. Furthermore, small angle X‐ray diffraction analyses demonstrate that myosin can bind to actin in an ATP‐dependent manner even after 9–14 days of exposure to CMV. Thus, quantitative changes in muscle fibre size and contractile proteins are not the dominating factors underlying the dramatic decline in diaphragm muscle function in response to CMV, in contrast to earlier observations in limb muscles. The observed early loss of subsarcolemmal neuronal nitric oxide synthase activity, onset of oxidative stress, intracellular lipid accumulation and post‐translational protein modifications strongly argue for significant qualitative changes in contractile proteins causing the severely impaired residual function in diaphragm fibres after long‐term mechanical ventilation. For the first time, the present study demonstrates novel changes in the diaphragm structure/function and underlying mechanisms at the gene, protein and cellular levels in response to CMV at a high temporal resolution ranging from 6 h to 14 days.

  • 93.
    Cui, Zhong-Kai
    et al.
    Department of Chemistry, Centre for Self-Assembled Chemical Structures (CSACS), Université de Montréal, Canada.
    Edwards, Katarina
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Orellana, Alejandro Nieto
    INSERM U1066, Micro et Nanomédecines Biomimétiques-MINT, France AND LUNAM Université, UMR-S1066, Angers F-49933, France.
    Bastiat, Guillaume
    INSERM U1066, Micro et Nanomédecines Biomimétiques-MINT, France AND LUNAM Université, UMR-S1066, Angers F-49933, France.
    Benoit, Jean-Pierre
    INSERM U1066, Micro et Nanomédecines Biomimétiques-MINT, France AND LUNAM Université, UMR-S1066, Angers F-49933, France.
    Lafleur, Michel
    Department of Chemistry, Centre for Self-Assembled Chemical Structures (CSACS), Université de Montréal, Canada.
    Impact of interfacial cholesterol-anchored polyethylene glycol on sterol-rich non-phospholipid liposomes2014In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 428, p. 111-120Article in journal (Refereed)
    Abstract [en]

    Hypothesis

    Liposomes made of single-chain amphiphiles and a large amount of sterols display several advantages including a limited permeability. In the present paper, we examine the possibility to prepare such non-phospholipid liposomes with interfacial polyethylene glycol (PEG) in order to improve their circulation in the blood stream. Cholesterol (Chol) was chosen as the PEG anchor.

    Experiments

    The phase behavior of mixtures of palmitic acid (PA) and cholesterol including various proportions of PEGylated cholesterol (PEG-Chol) was characterized. In conditions leading to the formation of fluid bilayers, properties of the resulting liposomes were assessed.

    Findings

    Up to 20 mol% of PEGylated cholesterol could be introduced without significant perturbations in fluid bilayers made of PA and cholesterol. With 10 mol% PEG-Chol, PA/Chol/PEG-Chol liposomes showed a very limited permeability to calcein and doxorubicin. Doxorubicin could be actively loaded in PA/Chol/PEG-Chol liposomes with a high drug loading efficiency and a high drug to lipid ratio. Pharmaco-kinetic experiments in rats indicated that interfacial PEG reduced the clearance of PA/Chol liposomes compared to the naked ones. However the lifetime of these non-phospholipid liposomes in the blood circulation was considerably shorter than that observed for control PEGylated phospholipid liposomes, a phenomenon associated with the negative interfacial charge of the PA/Chol/PEG-Chol liposomes. 

  • 94.
    da Silva, Marcelo A.
    et al.
    Institute of Pharmaceutical Science, King’s College London, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom.
    Weinzaepfel, Evelyne
    Institute of Pharmaceutical Science, King’s College London, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom.
    Afifi, Hala
    Institute of Pharmaceutical Science, King’s College London, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom.
    Eriksson, Jonny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Grillo, Isabelle
    Institut Laue-Langevin (ILL), DS/LSS, 6, rue Jules Horowitz, B.P. 156, 38042 Grenoble Cedex, France.
    Valero, Margarita
    Departamento de Química Física, Universidad de Salamanca, 37008 Salamanca, Spain.
    Dreiss, Cécile A.
    Institute of Pharmaceutical Science, King’s College London, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom.
    Tuning the Viscoelasticity of Nonionic Wormlike Micelles with beta-Cyclodextrin Derivatives: A Highly Discriminative Process2013In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 29, no 25, p. 7697-7708Article in journal (Refereed)
    Abstract [en]

    We report the influence of five β-cyclodextrin (β-CD) derivatives, namely: randomly methylated β-cyclodextrin (MBCD), heptakis (2,6-di-O-methyl)-β-cyclodextrin (DIMEB), heptakis (2,3,6-tri-O-methyl)-β-cyclodextrin (TRIMEB), 2-hydroxyethyl-β-cyclodextrin (HEBCD) and 2-hydroxypropyl-β-cyclodextrin (HPBCD), on the self-assembly of mixtures of nonionic surfactants: polyoxyethylene cholesteryl ether (ChEO10) and monocaprylin (MCL). Mixtures of ChEO10/MCL in water form highly viscoelastic wormlike micelle solutions (WLM) over a range of concentrations; herein, the composition was fixed at 10 wt % ChEO10/3 wt % MCL. The addition of methylated β-CDs (MBCD, DIMEB, TRIMEB) induced a substantial disruption of the solid-like viscoelastic behavior, as shown from a loss of the Maxwell behavior, a large reduction in G′ and G″ in oscillatory frequency-sweep measurements, and a drop of the viscosity. The disruption increased with the degree of substitution, following: MBCD < DIMEB < TRIMEB. Cryo-TEM images confirmed a loss of the WLM networks, revealing short rods and disc-like aggregates, which were corroborated by small-angle neutron scattering (SANS) measurements. Critical aggregation concentrations (CAC), measured by fluorescence spectroscopy, increased in the presence of DIMEB for both ChEO10 and MCL, suggesting the existence of interactions between methylated β-CDs and both surfactants involved in WLM formation. Instead, hydroxyl-β-CDs had a very different effect on the WLM. HPBCD only slightly reduced the solid-like behavior, without suppressing it. Quite remarkably, the addition of HEBCD reinforced the solid-like characteristics and increased the viscosity 10-fold. Cryo-TEM images confirmed the subsistence of WLM in ChEO10/MCL/HEBCD solutions, while SANS data revealed a slight elongation and thickening of the worms, and an increase of associated water molecules. CAC data showed that HPBCD had little effect on either surfactant, while HEBCD strongly affected the CAC of MCL and only slightly affected the ChEO10. For both DIMEB and HEBCD, time-resolved SANS measurements showed that morphology changes underlying these macroscopic changes occur in less than 100 ms.

  • 95.
    Dahlin, Andreas P
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Hjort, Klas
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Hillered, Lars
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Neurosurgery.
    Sjödin, Marcus O D
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Wetterhall, Magnus
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Quantification of Proteins Adsorbed to Surface Modified and Non-Modified Microdialysis Membranes using on-Surface Enzymatic Digestion (oSED) iTRAQ-MALDI-TOF/TOF MS2012In: 60th ASMS Conference on Mass Spectrometry and Allied Topics, May 20 - 24, Vancouver, Canada, 2012Conference paper (Refereed)
  • 96.
    Dahlin, Andreas P
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Hjort, Klas
    Uppsala University, Disciplinary Domain of Science and Technology, Technology, Department of Engineering Sciences, Microsystems Technology.
    Hillered, Lars
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Neurosurgery.
    Sjödin, Marcus O.D.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Wetterhall, Magnus
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Multiplexed quantification of proteins adsorbed to surface-modified and non-modified microdialysis membranes2012In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 402, no 6, p. 2057-2067Article in journal (Refereed)
    Abstract [en]

    A simple and straightforward method for discovery and quantification of proteins adsorbed onto delicate and sensitive membrane surfaces is presented. The adsorbed proteins were enzymatically cleaved while still adsorbed onto the membranes using an on-surface enzymatic digestion (oSED). This was followed by isobaric tagging, nanoliquid chromatography, and tandem mass spectrometry. Protein adsorption on tri-block copolymer Poloxamer 407 surface-modified microdialysis (MD) membranes were compared with protein adsorption on unmodified MD membranes. Ventricular cerebrospinal fluid (vCSF) kept at 37 °C was used as sample matrix. In total, 19 proteins were quantified in two biological replicates. The surface-modified membranes adsorbed 33% less proteins than control membranes and the most abundant proteins were subunits of hemoglobin and clusterin. The adsorption of clusterin on the modified membranes was on average 36% compared to control membranes. The most common protein in vCSF, Albumin, was not identified adsorbed to the surface at all. It was also experimentally verified that oSED, in conjunction with tandem mass spectrometry can be used to quantify femtomole amounts of proteins adsorbed on limited and delicate surfaces, such as MD membranes. The method has great potential and can be used to study much more complex protein adsorption systems than previously reported.

  • 97.
    De Conto, Charlène
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Effect of Ubiquinone and Solanesole on liposome behaviour under osotic stress2015Student paper second term, 10 credits / 15 HE creditsStudent thesis
  • 98.
    de Kock, Neil
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    A novel targeted analysis of peripheral steroids by ultra–performance supercritical fluid chromatography hyphenated to mass spectrometryIn: Article in journal (Other academic)
  • 99.
    de Kock, Neil
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    A novel ultra-performance supercritical fluid chromatography–tandem mass spectrometry method for separation of fourteen cholesterol oxidation productsManuscript (preprint) (Other academic)
  • 100.
    de Kock, Neil
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry.
    Mass spectrometry based analysis of endogenous sterols and hormones2018Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Bioanalytical applications using supercritical fluid chromatography (SFC) as analytical technique are of increasing interest. In essence, bioanalysis involves measurement of bioactive or endogenous compounds in biological matrices. SFC has emerged as an excellent choice for bioanalytical analysis, attributable to its speed, selectivity and efficiency compared with high performance liquid chromatography. Moreover, coupling of SFC with mass spectrometry (MS) provides the additional benefits of specificity and sensitivity.

    The aim of this thesis was to exploit these features by developing methods for the analysis of endogenous steroids, cholesterol oxidation products (COPs) and thyroid hormones (THs) by using ultra-performance supercritical fluid chromatography–tandem mass spectrometry (UPSFC–MS/MS) as analytical technique.

    Endogenous steroids control many physiological processes, including reproduction, maturation, gene expression and neurological functions in humans and animals. In the first study, three steroids were measured in domesticated White Leghorn (WL) chickens and ancestral Red Junglefowl (RJF) birds. Restraining stress caused a significantly larger increase in corticosterone levels in RJF than in WL, indicating a blunted hypothalamic–pituitary–adrenal (HPA) axis activity in domesticated chickens. The second study was a continuation of the first study and corticosterone levels from the F12 generation of an intercross between WL and RJF birds were measured before and after physical restraint stress. The expression levels of the glucocorticoid receptor (GR) in the hypothalamus and several genes in the adrenal glands were correlated with the post-stress levels of corticosterone in plasma. In the third study, the measurement of steroids was extended to assess more endogenous steroids from the four major classes, i.e. estrogens, androgens, progestogens and corticosterone.

    Endogenous COPs are of interest in pathophysiology. COPs are more readily disposed by cells than cholesterol. Therefore, cholesterol is oxidised to the more polar COPs and are generally more bioactive than cholesterol. Moreover, if their production in cells and tissues and/or their introduction with dietary animal fat are excessive, COPs could indeed contribute to the pathogenesis of various disease processes. Fourteen COPs were included in the fourth study and a novel method for their separation was developed.

    The last study in this thesis, involved the analysis of five THs. These hormones are vital for growth, developmental and metabolic processes of vertebrate life and play an important role in energy homeostasis. Measurements of circulating thyroid hormone levels are used in thyroid disorder diagnoses or treatment status monitoring. Two rapid methods for the separation of five THs were developed.

    In summary, the work in this thesis demonstrates the applicability of UPSFC–MS/MS as an analytical technique in bioanalysis of endogenous compounds.

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