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Issue 8, 2019
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Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's β-amyloid aggregation

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Abstract

The self-assembly of the beta-amyloid peptide (Aβ) into amyloid aggregates is a central phenomenon associated with Alzheimer's disease. Here, we report chemical modifications of key amino acid residues of Aβ42 (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 Aβ42.

Graphical abstract: Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's β-amyloid aggregation

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Publication details

The article was received on 22 Nov 2018, accepted on 03 Jan 2019 and first published on 03 Jan 2019


Article type: Communication
DOI: 10.1039/C8CC09288E
Chem. Commun., 2019,55, 1152-1155

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

    M. Ahn, B. I. Lee, S. Chia, J. Habchi, J. R. Kumita, M. Vendruscolo, C. M. Dobson and C. B. Park, Chem. Commun., 2019, 55, 1152
    DOI: 10.1039/C8CC09288E

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