Distinct impact of glycation towards the aggregation and toxicity of murine and human amyloid-ß.
Chem Commun (Camb)
; 57(62): 7637-7640, 2021 Aug 03.
Article
em En
| MEDLINE
| ID: mdl-34254069
ABSTRACT
Glycation of human Aß (hAß) is implicated to induce the deposition of amyloid aggregates found in the Alzheimer's disease (AD)-affected brain. Murine Aß (mAß) differs from hAß 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 mAß40 over hAß40 are distinctly generated. The different glycation between the two peptides can govern their aggregation kinetics, structural transition, and cytotoxicity.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos beta-Amiloides
/
Agregados Proteicos
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article