Abstracts of keynote & plenary lectures

• Publisher: Wiley (John Wiley & Sons)
• Year: 2005
• Tongue: English
• Weight: 141 KB
• Volume: 80
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.20320

✦ Synopsis

Identification of the secondary structure responsible for peptide biology is of academic interest to characterize natural modes of action, as well as industrially relevant for the development of peptide mimics. Traditionally, such scanning of peptide structure has been performed by systematic replacement of each residue in the peptide sequence with another proteinogenic amino acid. For example, alanine, enantiomeric amino acid and proline scans have been respectively performed to study the importance of side chains, stereochemistry and conformation on the biological activity of the peptide. Our lab has been developing alternative scanning methods for characterizing the relationship between peptide structure and activity. For example, we have recently introduced effective solid-phase methods for introducing aza-amino acid residues systematically at different positions along the peptide chain. Because aza-amino acid residues have been shown to adopt the i ϩ 1 and i ϩ 2 positions of beta-turns, aza-amino acid scanning offers potential for identifying regions of turn secondary structure which are important for biology. Similarly, we are pursuing solid-phase chemistry for introducing lactam constraints at different positions along the peptide. Our presentation will focus on recent achievements in the development of new methodology for scanning various peptide sequences to identify secondary structures relevant for biological activity.