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

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.