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

Item Type:Article
Title:Study of the conformational transition of Abeta(1-42) using D-amino acid replacement analogues
Creators Name:Janek, K. and Rothemund, S. and Gast, K. and Beyermann, M. and Zipper, J. and Fabian, H. and Bienert, M. and Krause, E.
Abstract: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.
Keywords:Amino Acid Sequence, Amino Acid Substitution, Amino Acids, Amyloid Beta-Protein, Biomolecular Nuclear Magnetic Resonance, Circular Dichroism, Electron Microscopy, Fourier Transform Infrared Spectroscopy, Light, Molecular Sequence Data, Peptide Fragments, Protein Conformation, Radiation Scattering, Secondary Protein Structure, Solvents, Thermodynamics, Trifluoroethanol
Source:Biochemistry
ISSN:0006-2960
Publisher:American Chemical Society (U.S.A.)
Volume:40
Number:18
Page Range:5457-5463
Date:1 January 2001
Official Publication:https://doi.org/10.1021/bi002005e
PubMed:View item in PubMed

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