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NMR study of five N-terminal peptide fragments of the vasoactive intestinal peptide: crucial role of aromatic residues.

作者信息

Goossens J F, Cotelle P, Chavatte P, Hénichart J P

机构信息

Institut de Chimie Pharmaceutique. Université de Lille II, France.

出版信息

Pept Res. 1996 Nov-Dec;9(6):322-6.

PMID:9048427
Abstract

Five peptides related to the N-terminal sequence of the vasoactive intestinal peptide (VIP) have been synthesized. Two-dimensional nuclear magnetic resonance (2D-NMR) experiments (i.e., correlated spectroscopy [COSY]) and low temperature coefficient measurements for particular NH chemical shifts suggest the presence of hydrogen bondings in both VIP (1-7, and VIP (1-11) fragments. Nuclear Over-hauser enhancement spectroscopy (NOESY) show that aromatic interactions stabilize a preferred conformation. The crucial role of the first histidine residue, which is a determinant for the biological activity, is explained by specific interactions with the aromatic protons of Phe6 and Tyr10.

摘要

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