Journal
BIOCHEMISTRY
Volume 40, Issue 18, Pages 5457-5463Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi002005e
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A critical event in Alzheimer's disease is the transition of A beta peptides from their soluble forms into disease-associated beta -sheet-rich conformers. Structural analysis of a complete D-amino acid replacement set of A beta (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 A beta (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.
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