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Analytical Approaches to Neurodegenerative Disease Protein Aggregation
KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
2011 (English)Licentiate thesis, comprehensive summary (Other academic)
Place, publisher, year, edition, pages
Stockholm: KTH Royal Institute of Technology , 2011. , vi, 38 p.
Trita-CHE-Report, ISSN 1654-1081 ; 2011:42
Keyword [en]
neurodegenerative diseases, protein misfolding, protein aggregation, gel electrophoresis, isoelectric focusing, immunodetection, ELISA, immunoprecipitation, mass spectrometry, nanoelectrospray, liquid chromatography
Keyword [sv]
neurodegenerativa sjukdomar, felveckade proteiner, proteinaggregering, geleektrofores, isoelektrisk fokusering, immundetektion, ELISA, immunoprecipitering, masspektrometri, nanoelektrospray, vätskekromatografi
National Category
Analytical Chemistry
URN: urn:nbn:se:kth:diva-34027ISBN: 978-91-7501-023-6 (print)OAI: diva2:418641
2011-06-15, Hörsal D2, KTH, Lindstedtsvägen 5, Stockholm, 13:00 (English)
QC 20110615Available from: 2011-06-15 Created: 2011-05-23 Last updated: 2011-06-16Bibliographically approved
List of papers
1. Separation and characterization of aggregated species of amyloid-beta peptides
Open this publication in new window or tab >>Separation and characterization of aggregated species of amyloid-beta peptides
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2010 (English)In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 397, no 6, 2357-2366 p.Article in journal (Refereed) Published
Abstract [en]

We have investigated the use of isoelectric focusing and immunodetection for the separation of low molecular weight species of amyloid-beta (A beta) peptides from their aggregates. From solutions of A beta(1-40) or A beta(1-42) monomeric peptides, low molecular weight material appeared at a pI value of ca. 5, while the presence of aggregates was detected as bands, observed at a pI of 6-6.5. The formation of A beta aggregates (protofibrils) was verified by a sandwich ELISA, employing the protofibril conformation-selective antibody mAb158. In order to study the aggregation behavior when using a mixture of the monomers, we utilized the IEF separation combined with Western blot using two polyclonal antisera, selective for A beta(1-40) and A beta(1-42), respectively. We conclude that both monomers were incorporated in the aggregates. In a further study of the mixed aggregates, we used the protofibril conformation-selective antibody mAb158 for immunoprecipitation, followed by nanoelectrospray mass spectrometry (IP-MS). This showed that the A beta(1-42) peptide is incorporated in the aggregate in a significantly larger proportion than its relative presence in the original monomer composition. IP-MS with mAb158 was also performed, and compared to IP-MS with the A beta-selective antibody mAb1C3, where a monomeric A beta(1-16) peptide was added to the protofibril preparation. A beta(1-16) is known for its poor aggregation propensity, and acted therefore as a selectivity marker. The results obtained confirmed the protofibril conformation selectivity of mAb158.

Alzheimer's disease, Protofibrils, Amyloid-beta (A beta), Isoelectric focusing (IEF)., Mass spectrometry (MS), Bioanalytical methods, Capillary electrophoresis / Electrophoresis
National Category
Analytical Chemistry
urn:nbn:se:kth:diva-26073 (URN)10.1007/s00216-010-3839-9 (DOI)000279453000038 ()2-s2.0-77955981824 (ScopusID)
6th International Conference on Instrumental Methods of Analysis Athens, GREECE, OCT 04-08, 2009
QC 20110214Available from: 2010-11-11 Created: 2010-11-11 Last updated: 2011-06-15Bibliographically approved
2. Differential kinetics of alpha-synuclein oligomer formation induced by 4-hydrozynonenal and 4-oxononeal
Open this publication in new window or tab >>Differential kinetics of alpha-synuclein oligomer formation induced by 4-hydrozynonenal and 4-oxononeal
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2011 (English)Manuscript (preprint) (Other academic)
National Category
Analytical Chemistry
urn:nbn:se:kth:diva-34783 (URN)
Available from: 2011-06-15 Created: 2011-06-15 Last updated: 2012-02-07Bibliographically approved

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