Disruption of the β-sheet structure of a protected pentapeptide, related to the β-amyloid sequence 17–21, induced by a single, helicogenic Cα-tetrasubstituted α-amino acid
✍ Scribed by Dr Fernando Formaggio; Andrea Bettio; Vittorio Moretto; Marco Crisma; Claudio Toniolo; Quirinus B. Broxterman
- Publisher
- John Wiley and Sons
- Year
- 2003
- Tongue
- English
- Weight
- 95 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.503
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✦ Synopsis
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, C^α^‐tetrasubstituted α‐amino acids) on the β‐sheet conformation adopted by a protected pentapeptide related to the sequence 17–21 of the β‐amyloid peptide. By use of FT‐IR absorption and ^1^H 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.