Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's beta-amyloid aggregation

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The self-assembly of the beta-amyloid peptide (A) into amyloid aggregates is a central phenomenon associated with Alzheimer's disease. Here, we report chemical modifications of key amino acid residues of A(42) (Y10, H13, H14, and M35) by photoexcited thioflavin-T (ThT), a fluorescent probe of amyloid structure. The quantitative chemical kinetics analysis shows that the oxidized monomer species does not self-assemble, nor perturb the aggregation kinetics of non-oxidized A beta(42).
Publisher
ROYAL SOC CHEMISTRY
Issue Date
2019-01
Language
English
Article Type
Article
Citation

CHEMICAL COMMUNICATIONS, v.55, no.8, pp.1152 - 1155

ISSN
1359-7345
DOI
10.1039/c8cc09288e
URI
http://hdl.handle.net/10203/251648
Appears in Collection
MS-Journal Papers(저널논문)
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