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| Item Type: | Article |
|---|---|
| Title: | Study of the conformational transition of Abeta(1-42) using D-amino acid replacement analogues |
| Creators Name: | Janek, K., Rothemund, S., Gast, K., Beyermann, M., Zipper, J., Fabian, H., 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 |
| 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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