Study of the conformational transition of A beta(1-42) using D-amino acid replacement analogues.

Abstract

A critical event in Alzheimer's disease is the transition of Abeta peptides from their soluble forms into disease-associated beta-sheet-rich conformers. Structural analysis of a complete D-amino acid replacement set of Abeta(1-42) enabled us to localize in the full-length 42-mer peptide the region responsible for the conformational switch into a beta-sheet structure. Although NMR spectroscopy of trifluoroethanol-stabilized monomeric Abeta(1-42) delineated two separated helical domains, only the destabilization of helix I, comprising residues 11-24, caused a transition to a beta-sheet structure. This conformational alpha-to-beta switch was directly accompanied by an aggregation process leading to the formation of amyloid fibrils.

050100150'03'05'07'09'11'13'15'17
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@article{Janek2001StudyOT, title={Study of the conformational transition of A beta(1-42) using D-amino acid replacement analogues.}, author={Katarina Janek and S Rothemund and Katrin Gast and Michael Beyermann and J . Zipper and Heinz Fabian and Michael Bienert and Eberhard Krause}, journal={Biochemistry}, year={2001}, volume={40 18}, pages={5457-63} }