Issue 62, 2021

Distinct impact of glycation towards the aggregation and toxicity of murine and human amyloid-β

Abstract

Glycation of human Aβ (hAβ) is implicated to induce the deposition of amyloid aggregates found in the Alzheimer's disease (AD)-affected brain. Murine Aβ (mAβ) differs from hAβ in three different amino acid residues (Gly5, Phe10, and Arg13) and is less likely to form amyloid aggregates. Herein, we report that the advanced glycated end products of mAβ40 over hAβ40 are distinctly generated. The different glycation between the two peptides can govern their aggregation kinetics, structural transition, and cytotoxicity.

Graphical abstract: Distinct impact of glycation towards the aggregation and toxicity of murine and human amyloid-β

Supplementary files

Article information

Article type
Communication
Submitted
22 май 2021
Accepted
28 юни 2021
First published
29 юни 2021

Chem. Commun., 2021,57, 7637-7640

Distinct impact of glycation towards the aggregation and toxicity of murine and human amyloid-β

E. Nam, J. Han, S. Choi and M. H. Lim, Chem. Commun., 2021, 57, 7637 DOI: 10.1039/D1CC02695J

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