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  • 1.
    Adbo, Karina
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ankarloo, Jonas
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Karlsson, Jesper G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Norell, M C
    Olofsson, Linus
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Svenson, Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Örtegren, U
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Enantioselective synthetic receptors for Tröger’s base1999In: Bioorganic Chemistry, Vol. 27, no 5, p. 363-371Article in journal (Refereed)
  • 2.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Karlsson, Jesper G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Piletsky, S A
    Koch-Schmidt, Ann-Christin
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Mosbach, K
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Influence of monomer-template ratio on selectivity and load capacity of molecularly imprinted polymers: indications of template self-association1999In: Journal of Chromatography A, Vol. 848, no 1-2, p. 39-49Article in journal (Refereed)
  • 3.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Karlsson, Jesper G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Svenson, Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Can template-template self-association contribute to polymer-ligand recognition characteristics?2000Conference paper (Refereed)
  • 4.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Koch-Schmidt, Ann-Christin
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Study of the Nature of Recognition in Molecularly Imprinted Polymers1996In: J. Mol. Recogn., Vol. 9, p 675-682Article in journal (Refereed)
  • 5.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Molecular Imprinting. Recent innovations in synthetic polymer receptor and enzyme mimics1997In: Recent Research Developments in Pure and Applied Chemistry, Vol. 1, p. 133-157Article in journal (Refereed)
  • 6.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Spectroscopic evaluation of molecular imprinting polymerization systems1997In: Bioorganic Chemistry, Vol. 25, p. 203-211Article in journal (Refereed)
  • 7.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    The development of molecular imprinting2000Other (Other academic)
  • 8.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Piletsky, S A
    Mosbach, K
    Koch-Schmidt, Ann-Christin
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Novel recognition elements for improved molecularly imprinted polymer stereoselectivity1997Conference paper (Refereed)
  • 9.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ramström, O
    Crown Ethers as a Tool for the Preparation of Molecularly Imprinted Polymers1998In: Journal of Molecular Recognition, Vol. 11, p. 103-106Article in journal (Refereed)
  • 10.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ramström, Olof
    Lund University.
    Crown ethers as a tool for the preparation of molecularly imprinted polymers1997Conference paper (Other academic)
  • 11. Andersson, L I
    et al.
    Nicholls, Ian Alan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Mosbach, K
    Immunoassays using molecularly imprinted polymers1995In: Immunoanalysis of agrochemicals: emerging technologies / [ed] Judd O. Nelson, Alexander E. Karu and Rosie B. Wong, American Chemical Society (ACS), 1995, p. 89-97Conference paper (Other academic)
  • 12.
    Bohman, Björn
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Cavonius, Lillie
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Unelius, C. Rikard
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Vegetables as biocatalysts in stereoselective hydrolysis of labile organic compounds2009In: Green Chemistry, ISSN 1463-9262, E-ISSN 1463-9270, Vol. 11, no 11, p. 1900-1905Article in journal (Refereed)
    Abstract [en]

    Hydrolysis of labile esters of beta-hydroxyketones has been performed with whole plant tissue from various vegetables. The pheromone 5-hydroxy-4-methyl-3-heptanone (1) was used as the model compound. Hydrolysis of acetates and benzoates of 1 was unsuccessful using normal conditions of ester hydrolysis, both by chemical hydrolysis and by the means of commercial lipases. When, however, whole cells of carrot, celery root, eggplant, parsley root, parsnip and potato were used as reagents, hydrolysis of the acetates was successful. At low conversion the hydrolysis was stereoselective and at total conversion virtually no formation of by-products was observed. The selectivity varied among the eight vegetables that were evaluated. Methods of preparation and substrate-to-plant ratio were examined. Furthermore, acetates and benzoates of three analogous compounds [5-hydroxy-3-heptanone (2), 5-hydroxy-5-methyl-3-heptanone (3) and 5-ethyl-6-hydroxy-4-octanone (4)] were hydrolyzed by potato and sweet potato to various degrees, indicating that the method is general for the mild and stereoselective hydrolysis of secondary beta-alkoxy-and beta-aryloxyketones.

  • 13.
    Bohman, Björn
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Unelius, C. Rikard
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Synthesis of all four stereoisomers of 5-hydroxy-4-methyl-3-heptanone using plants and oyster mushrooms2009In: Tetrahedron, ISSN 0040-4020, E-ISSN 1464-5416, Vol. 65, no 42, p. 8697-8701Article in journal (Refereed)
    Abstract [en]

    All four possible stereoisomers of 5-hydroxy-4-methyl-3-heptanone were synthesized from common achiral reagents using fast, straightforward organic synthesis, including the use of whole tissue of Daucus carota, Solanum melongena, and Pleurotus ostreatus.

  • 14. El-Sayed, Ashraf
    et al.
    Manning, Lee-Anne
    Unelius, C. Rikard
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Park, Kye-Chung
    Stringer, Lloyd
    White, Nicola
    Bunn, Barry
    Twidle, Andrew
    Suckling, Max
    Attraction and Antennal Response of the Common Wasp, Vespula vulgaris (L.), to Selected Synthetic Chemicals in New Zealand Beech Forests2009In: Pest Management Science, ISSN 1526-498X, E-ISSN 1526-4998, Vol. 65, no 9, p. 975-981Article in journal (Refereed)
    Abstract [en]

    BACKGROUND: The common wasp, Vespula vulgaris (L.), and the German wasp, Vespula germanica (F.), are significant problems in New Zealand beech forests (Nothofagus spp.), adversely affecting native birds and invertebrate biodiversity. This work was undertaken to develop synthetic attractants for these species to enable more efficient monitoring and management. RESULTS: Seven known wasp attractants (acetic acid, butyl butyrate, isobutanol, heptyl butyrate, octyl butyrate and 2,4-hexadienyl butyrate) were field tested, and only heptyl butyrate and octyl butyrate attracted significantly higher numbers of wasps than a non-baited trap. Accordingly, a series of straight-chain esters from methyl to decyl butyrate were prepared and field tested for attraction of social wasps. Peak biological activity occurred with hexyl butyrate, heptyl butyrate, octyl butyrate and nonyl butyrate. Polyethylene bags emitting approximately 18.4-22.6 mg day(-1) of heptyl butyrate were more attractive than polyethylene bags emitting approximately 14.7-16.8 mg day(-1) of heptyl butyrate in the field. Electroantennogram (EAG) studies indicated that queens and workers of V. vulgaris had olfactory receptor neurons responding to various aliphatic butyrates. CONCLUSION: These results are the first to be reported on the EAG response and the attraction of social wasps to synthetic chemicals in New Zealand beech forests and will enable monitoring of social wasp activity in beech forests. (C) 2009 Society of Chemical industry

  • 15. Göransson, Ulf
    et al.
    Herrmann, Anders
    Burman, Robert
    Haugaard-Kedström (published under the name Haugaard-Jönsson), Linda M.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Rosengren, K. Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    The conserved Glu in the cyclotide cycloviolacin O2 has a key structural role2009In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 10, no 14, p. 2354-2360Article in journal (Refereed)
    Abstract [en]

    Cyclotides are a large family of plant peptides that are characterised by a head-to-tail circular backbone and three disulfide bonds that are arranged in a cystine knot. This unique structural feature, which is referred to as a cyclic cystine knot, gives the cyclotides remarkable stability against chemical and biological degradation. In addition to their natural function as insecticides for plant defence, the cyclotides have a range of bioactivities with pharmaceutical relevance, including cytotoxicity against cancer cell lines. A glutamic acid residue, aside from the invariable disulfide array, is the most conserved feature throughout the cyclotide family, and it has recently been shown to be crucial for biological activity. Here we have used solution-state NMR spectroscopy to determine the three-dimensional structures of the potent cytotoxic cyclotide cycloviolacin O2, and an inactive analogue in which this conserved glutamic acid has been methylated. The structures of the peptides show that the glutamic acid has a key structural role in coordinating a set of hydrogen bonds in native cycloviolacin O2; this interaction is disrupted in the methylated analogue. The proposed mechanism of action of cyclotides is membrane disruption and these results suggest that the glutamic acid is linked to cyclotide function by stabilising the structure to allow efficient aggregation in membranes, rather than in a direct interaction with a target receptor.

  • 16.
    Haugaard-Kedström (published under the name Haugaard-Jönsson), Linda M.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Hossain, Akther
    Daly, Norelle
    Bathgate, Ross
    Craik, David
    Wade, John
    Rosengren, Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Structural characterization of a H3-INSL5 relaxin peptide chimera2007In: Proceedings of the 4th International Peptide Symposium / [ed] Wilce, Jackie, Cairns, Australia, 2007Conference paper (Refereed)
  • 17.
    Haugaard-Kedström (published under the name Haugaard-Jönsson), Linda M.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Hossain, M. Akhter
    Daly, Norelle L.
    Bathgate, Ross A.D.
    Wade, John D.
    Craik, David J.
    Rosengren, K. Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Structural Properties of Relaxin Chimeras: NMR Characterization of the R3/I5 Relaxin Peptide2009In: Annals of the New York Academy of Sciences, ISSN 0077-8923, E-ISSN 1749-6632, Vol. 1160, p. 27-30Article in journal (Refereed)
    Abstract [en]

    Relaxin-3 interacts with high potency with three relaxin family peptide receptors (RXFP1, RXFP3, and RXFP4). Therefore, the development of selective agonist and antagonist analogs is important for in vivo studies characterizing the biological significance of the different receptor-ligand systems and for future pharmaceutical applications. Recent reports demonstrated that a peptide selective for RXFP3 and RXFP4 over RXFP1 can be generated by the combination of the relaxin-3 B chain with the A chain from insulin-like peptide 5 (INSL5), creating an R3/I5 chimera. We have used NMR spectroscopy to determine the three-dimensional structure of this peptide to gain structural insights into the consequences of combining chains from two different relaxins. The R3/I5 structure reveals a similar backbone conformation for the relaxin-3 B chain compared to native relaxin-3, and the INSL5 A chain displays a relaxin/insulin-like fold with two parallel helices. The findings indicate that binding and activation of RXFP3 and RXFP4 mainly require the B chain and that the A chain functions as structural support. RXFP1, however, demonstrates a more complex binding mechanism, involving both the A chain and the B chain. The creation of chimeras is a promising strategy for generating new structure-activity data on relaxins.

  • 18.
    Haugaard-Kedström (published under the name Haugaard-Jönsson), Linda M.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Hossain, M. Akhter
    Daly, Norelle L.
    Craik, David J.
    Wade, John D.
    Rosengren, K. Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Structure of the human insulin-like peptide 5 and characterization of conserved hydrogen bonds and electrostatic interactions within the relaxin framework2009In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 419, p. 619-627Article in journal (Refereed)
    Abstract [en]

    INSL5 (insulin-like peptide 5) is a two-chain peptide hormone related to insulin and relaxin. It was recently discovered through searches of expressed sequence tag databases and, although the fulfil biological significance of INSL5 is still being elucidated, high expression in peripheral tissues such as the colon, as well as in the brain and hypothalamus, suggests roles in gut contractility and neuroendocrine signalling. INSL5 activates the relaxin family peptide receptor 4 with high potency and appears to be the endogenous ligand for this receptor, on the basis of overlapping expression profiles and their apparent co-evolution. In the present Study, we have used solution-state NMR to characterize the three-dimensional structure of synthetic human INSL5. The structure reveals an insulin/relaxin-like fold with three helical segments that are braced by three disulfide bonds and enclose a hydrophobic core. Furthermore, we characterized in detail the hydrogen-bond network and electrostatic interactions between charged groups in INSL5 by NMR-monitored temperature and pH titrations and Undertook a comprehensive structural comparison with other members of the relaxin family, thus identifying the conserved structural features of the relaxin fold. The B-chain helix, which is the primary receptor-binding site of the relaxins, is longer in INSL5 than in its close relative relaxin-3. As this feature results in a different positioning of the receptor-activation domain Arg(B23) and Trp(B24), it may be an important contributor to the difference in biological activity observed for these two peptides. Overall, the structural Studies provide mechanistic insights into the receptor selectivity of this important family of hormones. 

  • 19.
    Haugaard-Kedström (published under the name Haugaard-Jönsson), Linda M.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Hossain, Mohammed Akhter
    Daly, Norelle L.
    Bathgate, Ross A.D.
    Wade, John D.
    Craik, David J.
    Rosengren, Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Structure of the R3/I5 chimeric relaxin peptide, a selective GPCR135 and GPCR142 agonist2008In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 283, no 35, p. 23811-23818Article in journal (Refereed)
    Abstract [en]

    The human relaxin family comprises seven peptide hormones with various biological functions mediated through interactions with G-protein-coupled receptors. Interestingly, among the hitherto characterized receptors there is no absolute selectivity toward their primary ligand. The most striking example of this is the relaxin family ancestor, relaxin-3, which is an agonist for three of the four currently known relaxin receptors: GPCR135, GPCR142, and LGR7. Relaxin-3 and its endogenous receptor GPCR135 are both expressed predominantly in the brain and have been linked to regulation of stress and feeding. However, to fully understand the role of relaxin-3 in neurological signaling, the development of selective GPCR135 agonists and antagonists for in vivo studies is crucial. Recent reports have demonstrated that such selective ligands can be achieved by making chimeric peptides comprising the relaxin-3 B-chain combined with the INSL5 A-chain. To obtain structural insights into the consequences of combining A-and B-chains from different relaxins we have determined the NMR solution structure of a human relaxin-3/INSL5 chimeric peptide. The structure reveals that the INSL5 A-chain adopts a conformation similar to the relaxin-3 A-chain, and thus has the ability to structurally support a native-like conformation of the relaxin-3 B-chain. These findings suggest that the decrease in activity at the LGR7 receptor seen for this peptide is a result of the removal of a secondary LGR7 binding site present in the relaxin-3 A-chain, rather than conformational changes in the primary B-chain receptor binding site. 

  • 20. Hossain, M. Akhter
    et al.
    Bathgate, Ross A.D.
    Kong, Chze K.R.
    Shabanpoor, Fazel
    Zhang, Suode
    Haugaard-Kedström (published under the name Haugaard-Jönsson), Linda M.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Rosengren, Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Tregear, Geoffrey W.
    Wade, John D.
    Synthesis, conformation, and activity of human insulin-like peptide 5 (INSL5)2008In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 9, no 11, p. 1816-1822Article in journal (Refereed)
    Abstract [en]

    Insulin-like peptide 5 (INSL5) was first identified through searches of the expressed sequence tags (EST) databases. Primary sequence analysis showed it to be a prepropeptide that was predicted to be processed in vivo to yield a two-chain sequence (A and B) that contained the insulin-like disulfide cross-links. The high affinity interaction between INSL5 and the receptor RXFP4 (GPCR142) coupled with their apparent coevolution and partially overlapping tissue expression patterns strongly suggest that INSL5 is an endogenous ligand for RXFP4. Given that the primary function of the INSL5–RXFP4 pair remains unknown, an effective means of producing sufficient quantities of this peptide and its analogues is needed to systematically investigate its structural and biological properties. A combination of solid-phase peptide synthesis methods together with regioselective disulfide bond formation were used to obtain INSL5. Both chains were unusually resistant to standard synthesis protocols and required highly optimized conditions for their acquisition. In particular, the use of a strong tertiary amidine, DBU, as Nα-deprotection base was required for the successful assembly of the B chain; this highlights the need to consider incomplete deprotection rather than acylation as a cause of failed synthesis. Following sequential disulfide bond formation and chain combination, the resulting synthetic INSL5, which was obtained in good overall yield, was shown to possess a similar secondary structure to human relaxin-3 (H3 relaxin). The peptide was able to inhibit cAMP activity in SK-N-MC cells that expressed the human RXFP4 receptor with a similar activity to H3 relaxin. In contrast, it had no activity on the human RXFP3 receptor. Synthetic INSL5 demonstrates equivalent activity to the recombinant-derived peptide, and will be an important tool for the determination of its biological function.

  • 21. Hossain, M. Akhter
    et al.
    Bathgate, Ross A.D.
    Rosengren, K. Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Shabanpoor, Fazel
    Zhang, Suode
    Lin, Feng
    Tregear, Geoffrey W.
    Wade, John D.
    The structural and functional role of the B-chain C-terminal arginine in the relaxin-3 peptide antagonist, R3(B Delta 23-27)R/I5.2009In: Chemical Biology and Drug Design, ISSN 1747-0277, E-ISSN 1747-0285, Vol. 73, no 1, p. 46-52Article in journal (Refereed)
    Abstract [en]

    Relaxin-3, a member of the insulin superfamily, is involved in regulating stress and feeding behavior. It is highly expressed in the brain and is the endogenous ligand for the receptor RXFP3. As relaxin-3 also interacts with the relaxin receptor RXFP1, selective agonists and antagonists are crucial for studying the physiological function(s) of the relaxin-3/RXFP3 pair. The analog R3(B Delta 23-27)R/I5, in which a C-terminally truncated human relaxin-3 (H3) B-chain is combined with the INSL5 A-chain, is a potent selective RXFP3 antagonist and has an Arg residue remaining on the B-chain C-terminus as a consequence of the recombinant protein production process. To investigate the role of this residue in the RXFP3 receptor binding and activation, the analogs R3(B Delta 23-27)R/I5 and R3(B Delta 23-27)R containing the B-chain C-terminal Arg as well as R3(B Delta 23-27)/I5 and R3(B Delta 23-27), both lacking the Arg, were chemically assembled and their secondary structure and receptor activity assessed. The peptides generally had a similar conformation but those with the extra Arg residue displayed a significantly increased affinity for the RXFP3. Interestingly, in contrast to R3(B Delta 23-27)R and R3(B Delta 23-27)R/I5, the peptide R3(B Delta 23-27) is a weak agonist. This suggests that the C-terminal Arg, although increasing the affinity, alters the manner in which the peptide binds to the receptor and thereby prevents activation, giving R3(B Delta 23-27)R/I5 its potent antagonistic activity.

  • 22. Hossain, M. Akhter
    et al.
    Rosengren, Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Haugaard-Kedström (published under the name Haugaard-Jönsson), Linda M.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Zhang, Suode
    Layfield, Sharon
    Ferraro, Tania
    Daly, Norelle L.
    Tregear, Geoffrey W.
    Wade, John D.
    Bathgate, Ross A.D.
    The A-chain of the human relaxin family peptides has distinct roles in the binding and activation of the different relaxin family peptide receptors2008In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 283, no 25, p. 17287-17297Article in journal (Refereed)
    Abstract [en]

    The relaxin peptides are a family of hormones that share a structural fold characterized by two chains, A and B, that are cross-braced by three disulfide bonds. Relaxins signal through two different classes of G-protein-coupled receptors (GPCRs), leucine-rich repeat-containing GPCRs LGR7 and LGR8 together with GPCR135 and GPCR142, now referred to as the relaxin family peptide (RXFP) receptors 1-4, respectively. Although key binding residues have been identified in the B-chain of the relaxin peptides, the role of the A-chain in their activity is currently unknown. A recent study showed that INSL3 can be truncated at the N terminus of its A-chain by up to 9 residues without affecting the binding affinity to its receptor RXFP2 while becoming a high affinity antagonist. This suggests that the N terminus of the INSL3 A-chain contains residues essential for RXFP2 activation. In this study, we have synthesized A-chain truncated human relaxin-2 and -3 (H2 and H3) relaxin peptides, characterized their structure by both CD and NMR spectroscopy, and tested their binding and cAMP activities on RXFP1, RXFP2, and RXFP3. In stark contrast to INSL3, A-chain-truncated H2 relaxin peptides lost RXFP1 and RXFP2 binding affinity and concurrently cAMP-stimulatory activity. H3 relaxin A-chain-truncated peptides displayed similar properties on RXFP1, highlighting a similar binding mechanism for H2 and H3 relaxin. In contrast, A-chain-truncated H3 relaxin peptides showed identical activity on RXFP3, highlighting that the B-chain is the sole determinant of the H3 relaxin-RXFP3 interaction. Our results provide new insights into the action of relaxins and demonstrate that the role of the A-chain for relaxin activity is both peptide- and receptor-dependent. 

  • 23. Hossain, M. Akhter
    et al.
    Rosengren, K. Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Zhang, Suode
    Bathgate, Ross A.D.
    Tregear, Geoffrey W.
    van Lierop, Bianca J.
    Robinson, Andrea J.
    Wade, John D.
    Solid phase synthesis and structural analysis of novel A-chain dicarba analogs of human relaxin-3 (INSL7) that exhibit full biological activity2009In: Organic and biomolecular chemistry, ISSN 1477-0520, E-ISSN 1477-0539, Vol. 7, no 8, p. 1547-1553Article in journal (Refereed)
    Abstract [en]

    Replacement of disulfide bonds with non-reducible isosteres can be a useful means of increasing the in vivo stability of a protein. We describe the replacement of the A-chain intramolecular disulfide bond of human relaxin-3 (H3 relaxin, INSL7), an insulin-like peptide that has potential applications in the treatment of stress and obesity, with the physiologically stable dicarba bond. Solid phase peptide synthesis was used to prepare an A-chain analogue in which the two cysteine residues that form the intramolecular bond were replaced with allylglycine. On-resin microwave-mediated ring closing metathesis was then employed to generate the dicarba bridge. Subsequent cleavage of the peptide from the solid support, purification of two isomers and their combination with the B-chain via two intermolecular disulfide bonds, then furnished two isomers of dicarba-H3 relaxin. These were characterized by CD spectroscopy, which suggested a structural similarity to the native peptide. Additional analysis by solution NMR spectroscopy also identified the likely cis/trans form of the analogs. Both peptides demonstrated binding affinities that were equivalent to native H3 relaxin on RXFP1 and RXFP3 expressing cells. However, although the cAMP activity of the analogs on RXFP3 expressing cells was similar to the native peptide, the potency on RXFP1 expressing cells was slightly lower. The data confirmed the use of a dicarba bond as a useful isosteric replacement of the disulfide bond.

  • 24.
    Karlsson, Björn C. G.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    O'Mahony, John
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Karlsson, Jesper G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Bengtsson, Helen
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Eriksson, Leif A
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Structure and Dynamics of Monomer-Template Complexation: An Explanation for Molecularly Imprinted Polymer Recognition Site Heterogeneity2009In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 131, no 37, p. 13297-13304Article in journal (Refereed)
    Abstract [en]

    We here present the first simulation of a complete molecularly imprinted polymer prepolymerization system. Molecular dynamics studies were performed for a system comprising a total of 1199 discrete molecules, replicating the components and concentrations employed in the corresponding polymer synthesis. The observed interactions correlate well with results obtained from (1)H NMR spectroscopic studies. Comparison with simulations performed in the absence of cross-linking agent (ethylene dimethacrylate) demonstrated its significance in the formation of ligand recognition sites. Moreover, the influence of events such as template-template (bupivacaine) and monomer-monomer (methacrylic acid) self-association, porogen-template interactions, and template conformational variability was revealed. The template recognition capacity of the modeled polymer system was verified by synthesis of imprinted and reference polymers and subsequent radioligand binding Analysis. Collectively, through a series of statistical analyses of molecular trajectories in conjunction with spectroscopic data it was demonstrated that an ensemble of complex structures is present in the prepolymerization mixture and that this diversity is the basis for the binding site heterogeneity observed in molecularly imprinted polymers (MIPs) prepared using the noncovalent strategy.

  • 25.
    Karlsson, Björn C. G.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Rosengren, Annika M.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Per Ola
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Molecular Insights on the Two Fluorescence Lifetimes Displayed by Warfarin from Fluorescence Anisotropy and Molecular Dynamics Studies2009In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 113, no 22, p. 7945-7949Article in journal (Refereed)
    Abstract [en]

    A series of steady-state fluorescence anisotropy experiments has been performed to demonstrate the presence of a deprotonated open side chain form of warfarin in organic environments. We explain the observed emission-wavelength-dependent anisotropy of warfarin in ethanol, 2-propanol, and acetonitrile due to the coexistence of neutral isomers and deprotonated open side chain forms displaying different fluorescence decay kinetics. To investigate solvent-solute interactions in more detail, a series of molecular dynamics simulations was performed to study warfarin solvation and to predict the time scale of rotational diffusion displayed by this compound. Predictions obtained provide an explanation for the nonzero values in anisotropy observed for neutral isomers of warfarin associated with the short fluorescence lifetime (tau < 0.1 ns) and for an approximately zero anisotropy observed for the deprotonated open side chain form, which is associated with the longer fluorescence lifetime (tau = 0.5-1.6 ns). Finally, we address the potential use of fluorescence anisotropy for an increased understanding of the structural diversity of warfarin in protein binding pockets.

  • 26.
    Karlsson, Björn
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    O'Mahony, John
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Karlsson, Jesper G
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Bengtsson, Helen
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Eriksson, Leif A
    Nicholls, Ian Alan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Structure and dynamics of monomer-template complexation: an explanation for molecularly imprinted polymer recognition site heterogeneity2008Conference paper (Other academic)
  • 27.
    Kirsch, Nicole
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Hedin-Dahlström, Jimmy
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Henschel, Henning
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Whitcombe, Michael J
    Wikman, Susanne
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Molecularly imprinted polymer catalysis of a Diels-Alder reaction2009In: Journal of Molecular Catalysis B: Enzymatic, ISSN 1381-1177, E-ISSN 1873-3158, Vol. 58, no 1-4, p. 110-117Article in journal (Refereed)
    Abstract [en]

    A series of synthetic polymers were designed and synthesized for enhancing the rate of the Diels-Alder cycloaddition reaction of 1,3-butadiene carbamic acid benzyl ester (11) and N,N-dimethyl acrylamide (2), to yield the corresponding endo- (3) and exo- (4) reaction products. Putative transition state analogues (TSAs) for the endo- (5) and exo- (6) reaction pathways were used as templates for the synthesis of molecularly imprinted methacrylic acid (MAA)-divinylbenzene (DVB) copolymers. The polymer system utilized was selected based upon a series of (1)H NMR studies of complex formation between template and a functional monomer analogue (K(d) (app) approximate to 70 mM, d(8)-toluene, 293 K). Batch binding studies revealed that the imprinted polymers were selective for the TSA corresponding to the template used in the polymer synthesis. Studies on the influence of the polymers on the catalysis of the reaction of 1 and 2 demonstrated a 20-fold enhancement of the rate of the reaction relative to the solution reaction. A surprising temperature dependence of the reaction of 1 and 2 in the presence of the polymers was observed, which provides support for the role of template-functional monomer complexes in the catalysis of the Diels-Alder reaction.

  • 28. Knutsson, M
    et al.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Novel chiral recognition elements for molecularly imprinted polymer preparation1998In: Journal of Molecular Recognition, Vol. 11, p. 87-90Article in journal (Refereed)
  • 29.
    Månsson, Alf
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Balaz, Martina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Torres, Nuria Albet
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Rosengren, Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    In vitro assays of molecular motors - impact of motor-surface interactions2008In: Frontiers in Bioscience, ISSN 1093-9946, E-ISSN 1093-4715, Vol. 13, no May 1, p. 5732-5754Article, review/survey (Other academic)
    Abstract [en]

    In many types of biophysical studies of both single molecules and ensembles of molecular motors the motors are adsorbed to artificial surfaces. Some of the most important assay systems of this type (in vitro motility assays and related single molecule techniques) will be briefly described together with an account of breakthroughs in the understanding of actomyosin function that have resulted from their use. A poorly characterized, but potentially important, entity in these studies is the mechanism of motor adsorption to surfaces and the effects of motor surface interactions on experimental results. A better understanding of these phenomena is also important for the development of commercially viable nanotechnological applications powered by molecular motors. Here, we will consider several aspects of motor surface interactions with a particular focus on heavy meromyosin (HMM) from skeletal muscle. These aspects will be related to heavy meromyosin structure and relevant parts of the vast literature on protein-surface interactions for non-motor proteins. An overview of methods for studying motor-surface interactions will also be given. The information is used as a basis for further development of a model for HMM-surface interactions and is discussed in relation to experiments where nanopatterning has been employed for in vitro reconstruction of actomyosin order. The challenges and potentials of this approach in biophysical studies, compared to the use of self-assembly of biological components into supramolecular protein aggregates (e. g. myosin filaments) will be considered. Finally, this review will consider the implications for further developments of motor-powered lab-on-a-chip devices.

  • 30.
    Nicholls, Ian A.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Adbo, Karina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Per-Ola
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ankarloo, Jonas
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Hedin-Dahlström, Jimmy
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Jokela, Päivi
    University of Kalmar, School of Communication and Design.
    Karlsson, Jesper G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Olofsson, Linus
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Rosengren-Holmberg, Jenny
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Shoravi, Siamak
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Svenson, Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Wikman, Susanne
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Can we rationally design molecularly imprinted polymers?2001In: Analytica Chimica Acta, Vol. 435, no 1, p. 9-18Article in journal (Refereed)
  • 31.
    Nicholls, Ian A.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Thermodynamic principles underlying molecularly imprinted polymer formation and ligand recognition2000Other (Other academic)
  • 32.
    Nicholls, Ian A.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Charlton, Christy
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Henschel, Henning
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Karlsson, Björn C. G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Karlsson, Jesper G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    O'Mahony, John
    Rosengren, Annika M.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Rosengren, K. Johan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Wikman, Susanne
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Theoretical and Computational Strategies for Rational Molecularly Imprinted Polymer Design2009In: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 25, no 3, p. 543-552Article in journal (Refereed)
    Abstract [en]

    The further evolution of molecularly imprinted polymer science and technology necessitates the development of robust predictive tools capable of handling the complexity of molecular imprinting systems. A combination of the rapid growth in computer power over the past decade and significant software developments have opened new possibilities for simulating aspects of the complex molecular imprinting process. We present here a survey of the current status of the use of in silico-based approaches to aspects of molecular imprinting. Finally, we highlight areas where ongoing and future efforts should yield information critical to our understanding of the underlying mechanisms sufficient to permit the rational design of molecularly imprinted polymers. 

  • 33.
    Nicholls, Ian A.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Per-Ola
    Karlsson, Björn C. G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Rosengren, Annika M.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Method and apparatus for detecting pharmaceuticals in a sample2009Patent (Other (popular science, discussion, etc.))
  • 34.
    Nicholls, Ian A.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nilsson Ekdahl, Kristina
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Moledcular Imprints2009Patent (Other (popular science, discussion, etc.))
  • 35.
    Nicholls, Ian Alan
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Piletsky, Sergey A.
    Chen, Biening
    Chianella, Iva
    Turner, Anthony P. F.
    Thermodynamic considerations and the use of molecular modeling as a tool for predicting MIP performance2005In: Molecularly imprinted materials: science and technology / [ed] Mingdi Yan and Olof Ramström, New York: Marcel Dekker, 2005, 1, p. 363-393Chapter in book (Other academic)
  • 36. Norell, M S
    et al.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Theophylline molecularly imprinted polymer dissociation kinetics: A novel sustained release drug dosage mechanism1998In: Journal of Molecular Recognition, Vol. 11, p. 98-102Article in journal (Refereed)
  • 37.
    Olofsson, Linus
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Söderberg, Pernilla
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ankarloo, Jonas
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian Alan
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Phage display screening in low dielectric media2008In: Journal of Molecular Recognition, ISSN 0952-3499, E-ISSN 1099-1352, Vol. 21, no 5, p. 330-337Article in journal (Refereed)
    Abstract [en]

    Here we report the first application of phage display screening in low dielectric media. Two series of phage clones with affinity for α-chymotrypsin (CT) were selected from a Ph.D.TM-C7C library, using either a buffer or acetonitrile in buffer (50%, v/v). The affinity of lysates, individual clones or selected cyclic peptides for the enzyme was studied by examining their influence on CT activity. Peptides displayed on phage selected in buffer provided significant protection from enzyme autolysis resulting in marked increase in CT activity (>100%). Phage selected in ACN provided some, albeit weak, protection from the detrimental influence on CT from ACN. In conclusion, the results demonstrate the potential for the application of phage display screening protocols to targets in media of low dielectricity.

  • 38. Petcu, Mira
    et al.
    Karlsson, Jesper G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Whitcombe, M J
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Probing the limits of molecular imprinting: strategies with a template of limited size and functionality2009In: Journal of Molecular Recognition, ISSN 0952-3499, E-ISSN 1099-1352, Vol. 22, no 1, p. 18-25Article in journal (Refereed)
    Abstract [en]

    A series of polymers molecularly imprinted with the general anaesthetic propofol were synthesized using both semi- and non-covalent approaches. The polymers were evaluated with respect to template rebinding in both aqueous and organic media. In aqueous media, the observed propofol binding in these polymer systems was largely hydrophobic and non-specific in nature. In non-polar solvents such as hexane, electrostatic (hydrogen bonding) interactions dominate resulting in some selectivity. The implication of these results, in conjunction with those obtained using structures of similar size in other studies, is that propofol, a template possessing limited functionality and size, appears to define the lower limit for template size and degree of functionalization that can be used for the creation of ligand-selective recognition sites in molecularly imprinted polymers. Furthermore, studies with alternative ligands indicate that the steric crowding of a ligand's functionality to the polymer contributes to the extent of polymer-ligand recognition.

  • 39. Piletsky, S A
    et al.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    A new approach to molecularly imprinted polymer preparation1997Conference paper (Refereed)
  • 40. Piletsky, S A
    et al.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Combined hydrophobic and electrostatic interaction based recognition in molecularly imprinted polymers1999In: Macromolecules, Vol. 32, p. 633-636Article in journal (Refereed)
  • 41. Piletsky, S A
    et al.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    The rational use of the hydrophobic effect and electrostatic interaction based recognition in molecularly imprinted polymers1998In: Journal of Molecular Recognition, Vol. 11, p. 94-97Article in journal (Refereed)
  • 42. Piletsky, S A
    et al.
    Terpetschnig, E
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Wolfbeis, O S
    Application of non-specific fluorescent dyes for monitoring enantio-selective ligand-polymer binding in molecularly imprinted polymers1999In: Fresenius Journal of Analytical Chemistry, Vol. 364, p. 512-516Article in journal (Refereed)
  • 43.
    Rosengren, Annika M.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Golker, Kerstin
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Karlsson, Jesper G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Dielectric constants are not enough: Principal component analysis of the influence of solvent properties on molecularly imprinted polymer–ligand rebinding2009In: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 25, no 3, p. 553-557Article in journal (Refereed)
    Abstract [en]

    The influence of the physical properties of incubation medium on the rebinding of template to bupivacaine molecularly imprinted and non-imprinted methacrylic acid–ethylene dimethacrylate co-polymers has been studied. Principal component analysis (PCA) was employed to identify the factors with the greatest influence on binding. While the dielectric constant (D) made a significant contribution to describing the observed binding, the influence of polarity as reflected in the Snyder polarity index (SPI) was also demonstrated to make a significant contribution. The use of solvents containing hydroxyl functionality in particular was observed to exert unique effects on recognition. The variation in solvent influence on binding at constant D motivates more complex analyses when studying MIP–ligand recognition.

  • 44.
    Rosengren, Johan
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Bathgate, Ross
    Craik, David
    Daly, Norelle
    Haugaard-Kedström (published under the name Haugaard-Jönsson), Linda M.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Hossain, Akther
    Lin, Feng
    Wade, John
    Structural insights into the action of relaxin peptide hormones2007In: Proceedings of the 4th International Peptide Symposium / [ed] Wilce, Jackie, Cairns, Australia, 2007Conference paper (Refereed)
  • 45.
    Rosengren, Johan
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Daly, N L
    Fornander, L M
    Haugaard-Kedström (published under the name Jönsson), Linda M.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Shirafuji, Y
    Qu, X Q
    Vogel, H J
    Ouellette, A J
    Craik, D J
    Structural and functional characterization of the conserved salt bridge in mammalian Paneth cell alpha-defensins - Solution structures of mouse cryptdin-4 AND (E15D)-cryptdin-42006In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 281, no 38, p. 28068-28078Article in journal (Refereed)
    Abstract [en]

    alpha-Defensins are mediators of mammalian innate immunity, and knowledge of their structure-function relationships is essential for understanding their mechanisms of action. We report here the NMR solution structures of the mouse Paneth cell alpha-defensin cryptdin-4 (Crp4) and a mutant (E15D)-Crp4 peptide, in which a conserved Glu(15) residue was replaced by Asp. Structural analysis of the two peptides confirms the involvement of this Glu in a conserved salt bridge that is removed in the mutant because of the shortened side chain. Despite disruption of this structural feature, the peptide variant retains a well defined native fold because of a rearrangement of side chains, which result in compensating favorable interactions. Furthermore, salt bridge-deficient Crp4 mutants were tested for bactericidal effects and resistance to proteolytic degradation, and all of the variants had similar bactericidal activities and stability to proteolysis. These findings support the conclusion that the function of the conserved salt bridge in Crp4 is not linked to bactericidal activity or proteolytic stability of the mature peptide.

  • 46.
    Rosengren, K. Johan
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Bathgate, Ross A.D.
    Craik, David J.
    Daly, Norelle L.
    Haugaard-Kedström (published under the name Haugaard-Jönsson), Linda M.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Hossain, M. Akhter
    Wade, John D.
    Structural insights into the function of relaxins2009In: Annals of the New York Academy of Sciences, ISSN 0077-8923, E-ISSN 1749-6632, Vol. 1160, p. 20-26Article in journal (Refereed)
    Abstract [en]

    The relaxin peptide hormones are members of the insulin superfamily and share a structural fold that is characterized by two peptide chains which are cross-braced by three disulfide bonds. On this framework, various amino acid side chains are presented, allowing specific interactions with different receptors. The relaxin receptors belong to two unrelated classes of G-protein-coupled receptors, but interestingly they are not selective for a single relaxin peptide. Relaxin-3, which is considered to be an extreme example of the relaxin family, can activate receptors from both classes and in fact interacts to some degree with all four receptors identified to date. To deduce how changes in the primary sequence can fine-tune the overall structure and thus the ability to interact with the various receptors, we have studied a range of relaxin-like peptides using solution nuclear magnetic resonance analysis. Three-dimensional structures of relaxin-3, insulin-like peptide 3 (INSL3), and INSL5 were determined and revealed a number of interesting features. All peptides showed a significant amount of line-broadening in certain regions, in particular around the intra-A-chain disulfide bond, suggesting that despite the disulfide bonds the fold is rather dynamic. Although the peptides share a common structural core there are significant differences, particularly around the termini. The structural data in combination with mutational studies provide valuable insights into the structure-activity relationships of relaxins.

  • 47.
    Rosengren-Holmberg, Jenny P.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Karlsson, Jesper G.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Svenson, Johan
    Andersson, Håkan S.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Synthesis and ligand recognition of paracetamol selective polymers: semi-covalent versus non-covalent molecular imprinting.2009In: Organic and biomolecular chemistry, ISSN 1477-0520, E-ISSN 1477-0539, Vol. 7, p. 3148-3155Article in journal (Refereed)
    Abstract [en]

    Three molecular imprinting strategies, each based upon a series of ethylene glycol dimethacrylate (EGDMA) cross-linked co-polymers, have been used to produce materials selective for the commonly used analgesic and antipyretic agent paracetamol (p-acetaminophen or 4-acetamidophenol) (1). The polymers were synthesised using either a semi-covalent imprinting strategy based upon 4-acetamidophenyl-(4-vinylphenyl) carbonate (4) or a non-covalent strategy based on methacrylic acid (MAA) as the functional monomer, or by employing a combination of these strategies. Radioligand binding studies demonstrated low template affinity in polymers offering only a single electrostatic interaction point for recognition via the phenolic residue in the template, whereas binding was substantially increased upon the introduction of a second binding mode, namely interaction at the acetamide moiety. HPLC analyses revealed no imprinting effect in the purely semi-covalent system, and only a minor effect in the purely non-covalent systems. However, a pronounced imprinting effect was demonstrated for polymers prepared by a combination of semi-covalent and non-covalent imprinting. This study illustrates a limitation of both the non-covalent and the semi-covalent strategies when it comes to achieving imprinted selectivity for small and poorly functionalised templates such as paracetamol. Parallels with conclusions from studies with antibodies are discussed. 

  • 48. Strandh, Magnus
    et al.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Weak Affinity Chromatography2000Book (Other academic)
  • 49.
    Svenson, Johan
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Piletsky, S A
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Spectroscopic studies of the molecular imprinting self assembly process1997Conference paper (Refereed)
  • 50.
    Svenson, Johan
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Håkan S.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Piletsky, S A
    Nicholls, Ian A.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Spectroscopic studies of the molecular imprinting self assembly process1998In: Journal of Molecular Recognition, Vol. 11, p. 83-86Article in journal (Refereed)
12 1 - 50 of 53
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