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 ሜይ 2021
Accepted
28 ጁን 2021
First published
29 ጁን 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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements