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- Title
Disruption of the β-sheet structure of a protected pentapeptide, related to the β-amyloid sequence 1721, induced by a single, helicogenic C<sup>α</sup>-tetrasubstituted α-amino acid.
- Authors
Fernando Formaggio; Andrea Bettio; Vittorio Moretto; Marco Crisma; Claudio Toniolo; Quirinus B. Broxterman
- Abstract
Fifteen years ago it was shown that an α-aminoisobutyric acid (Aib) residue is significantly more effective than an L-Pro or a D-amino acid residue in inducing β-sheet disruption in short model peptides. As this secondary structure element is known to play a crucial role in the neuropathology of Alzheimer's disease, it was decided to check the effect of Aib (and other selected, helix inducer, Cα-tetrasubstituted α-amino acids) on the β-sheet conformation adopted by a protected pentapeptide related to the sequence 1721 of the β-amyloid peptide. By use of FT-IR absorption and 1H NMR techniques it was found that the strong self-association characterizing the pentapeptide molecules in weakly polar organic solvents is completely abolished by replacing a single residue with Aib or one of its congeners. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.
- Subjects
AMINO acids; ORGANIC acids; PEPTIDES; NEUROLOGICAL disorders; ALZHEIMER'S disease
- Publication
Journal of Peptide Science, 2003, Vol 9, Issue 7, p461
- ISSN
1075-2617
- Publication type
Article
- DOI
10.1002/psc.503