Determination of Peptide oligomerization state using rapid photochemical crosslinking

The assembly of the amyloid beta-protein (Abeta) into neurotoxic oligomers and fibrils is a seminal pathogenic process in Alzheimer's disease (AD). Understanding the mechanisms of Abeta assembly could prove useful in the identification of therapeutic targets. Owing to the metastable nature of A...

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Bibliographic Details
Published inMethods in molecular biology (Clifton, N.J.) Vol. 299; p. 11
Main Authors Vollers, Sabrina S, Teplow, David B, Bitan, Gal
Format Journal Article
LanguageEnglish
Published United States 2005
Subjects
Amyloid beta-Peptides - analysis
Amyloid beta-Peptides - chemistry
Organometallic Compounds
Photochemistry - instrumentation
Photochemistry - methods
Photolysis
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Summary:The assembly of the amyloid beta-protein (Abeta) into neurotoxic oligomers and fibrils is a seminal pathogenic process in Alzheimer's disease (AD). Understanding the mechanisms of Abeta assembly could prove useful in the identification of therapeutic targets. Owing to the metastable nature of Abeta oligomers, it is difficult to obtain interpretable data through application of classical methods, such as electrophoresis, chromatography, fluorescence, and light scattering. Here, we apply the method Photo-Induced Crosslinking of Unmodified Proteins (PICUP) to the study of Abeta oligomerization. This method directly produces covalent bonds among unmodified polypeptide chains through in situ generation of peptide free radicals. PICUP provides a snapshot of the native oligomerization state of proteins and can be used for assembly state analysis of a wide variety of peptides and proteins.
ISSN:1064-3745
DOI:10.1385/1-59259-874-9:011