Header menu link for other important links
Introduction of d-Glutamate at a Critical Residue of Aβ42 Stabilizes a Prefibrillary Aggregate with Enhanced Toxicity
C.J.A. Warner, , A.R. Foley, J.A. Raskatov
Published in Wiley-VCH Verlag
PMID: 27272258
Volume: 22
Issue: 34
Pages: 11967 - 11970
The amyloid beta peptide 42 (Aβ42) is an aggregation-prone peptide that plays a pivotal role in Alzheimer′s disease. We report that a subtle perturbation to the peptide through a single chirality change at glutamate 22 leads to a pronounced delay in the β-sheet adoption of the peptide. This was accompanied by an attenuated propensity of the peptide to form fibrils, which was correlated with changes at the level of the fibrillary architecture. Strikingly, the incorporation of d-glutamate was found to stabilize a soluble, ordered macromolecular assembly with enhanced cytotoxicity to PC12 cells, highlighting the importance of advanced prefibrillary Aβ aggregates in neurotoxicity. © 2016 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.
About the journal
JournalData powered by TypesetChemistry - A European Journal
PublisherData powered by TypesetWiley-VCH Verlag