Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously

✍ Scribed by David Pantoja-Uceda; M. Teresa Pastor; Jesús Salgado; Antonio Pineda-Lucena; Enrique Pérez-Payá

• Book ID: 105359652
• Publisher: John Wiley and Sons
• Year: 2008
• Tongue: English
• Weight: 537 KB
• Volume: 14
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.1015

✦ Synopsis

Abstract

This article describes a strategy to develop, starting from a de novo design, bivalent peptides containing two different (α‐helix and β‐hairpin) and independent secondary‐structure elements. The design was based on the use of conformationally restricted peptide libraries. Structural characterization by NMR revealed that the peptides were stable and did not show any long‐range NOE interactions between the N‐terminal β‐hairpin and the C‐terminal α‐helix. These results suggest that the two elements of secondary structure are stable and well folded. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.