Conformational Studies on Potential β-Turn-Forming Model Peptides

✍ Scribed by Karsten Bode; Murray Goodman; Manfred Mutter

• Book ID: 102856820
• Publisher: John Wiley and Sons
• Year: 1985
• Tongue: German
• Weight: 577 KB
• Volume: 68
• Category: Article
• ISSN: 0018-019X
• DOI: 10.1002/hlca.19850680320

✦ Synopsis

Abstract

The conformational behavior of POE‐bound model peptides Boc‐(L‐Ala)~2~‐X‐Y‐(L‐Ala)~2~‐NHPOE (X – Y = L‐Pro‐Gly (I), Gly‐L‐Ile (II); NHPOE = aminopoly(oxyethylene)) as well as of the repetitive hexapeptide of elastin, Boc‐L‐Val‐L‐Ala‐L‐Pro‐Gly‐L‐Val‐Gly‐A‐NHPOE‐M (III) (A = photosensitive 3‐nitro‐4‐(bromomethyl)benzoyl group; NHPOE‐M = aminopoly(oxyethylane) monomethyl ether) has been studied by means of ^1^H‐NMR and CD spectroscopy. Compounds I and III form a β‐turn with Pro and Gly in positions i + 1 and i + 2, respectively, while an aggregated state for II, has been identified. The results are in good agreement with published prediction codes giving experimental evidence for the dominance of short‐range interactions to establish secondary structure in solution.