Peptides containing the sulfonamide junction: Synthesis, structure, and conformation of Z-Tau-Pro-Phe-NHiPr

✍ Scribed by A. Calcagni; D. Rossi; M. Paglialunga Paradisi; G. Lucente; G. Luisi; E. Gavuzzo; F. Mazza; G. Pochetti; M. Paci

• Publisher: Wiley (John Wiley & Sons)
• Year: 1997
• Tongue: English
• Weight: 183 KB
• Volume: 41
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(19970415)41:5<555::aid-bip7>3.0.co;2-l

✦ Synopsis

The taurine (Tau) containing tripeptide derivative Z-Tau-Pro-Phe-NHiPr (1) has been synthesized as suitable sulfonamido-pseudopeptide model to investigate formation and conformational properties of folded secondary structures stabilized by intramolecular H bonds directly involving the sulfonamide junction. In the crystal the pseudopeptide 1 adopts a type I b-turn with the Pro and Phe residues located at the (i / 1) and (i / 2) corner positions, respectively. The turn is stabilized by a 4 r 1 H bond engaging one of the SO 2 oxygen atoms and the isopropylamide NH. In CDCl 3 solution the b-turn folding is accompanied by a g-turn centered at the Pro and involving a 3 r 1 H bond between the SO 2 and the Phe NH.