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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Janek K,Rothemund S,Gast K,Beyermann M,Zipper J,Fabian H,Bienert M,Krause Edoi
10.1021/bi002005esubject
Has Abstractpub_date
2001-05-08 00:00:00pages
5457-63issue
18eissn
0006-2960issn
1520-4995pii
bi002005ejournal_volume
40pub_type
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