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

Cited 0 time in webofscience Cited 0 time in scopus
  • Hit : 164
  • Download : 0
Glycation of human A beta (hA beta) is implicated to induce the deposition of amyloid aggregates found in the Alzheimer's disease (AD)-affected brain. Murine A beta (mA beta) differs from hA beta 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 mA beta(40) over hA beta(40) are distinctly generated. The different glycation between the two peptides can govern their aggregation kinetics, structural transition, and cytotoxicity.
Publisher
ROYAL SOC CHEMISTRY
Issue Date
2021-08
Language
English
Article Type
Article
Citation

CHEMICAL COMMUNICATIONS, v.57, no.62, pp.7637 - 7640

ISSN
1359-7345
DOI
10.1039/d1cc02695j
URI
http://hdl.handle.net/10203/287221
Appears in Collection
CH-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0