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Keywords:

  • dehydropentapeptides;
  • nuclear magnetic resonance;
  • circular dichroism;
  • X-ray crystallography;
  • β-bend;
  • hydrogen bond;
  • 310-helical conformation;
  • oligopeptides

Abstract

The structures of two dehydropentapeptides, Boc–Pro–ΔPhe–Val–ΔPhe–Ala–OMe (I) and Boc–Pro–ΔPhe–Gly–ΔPhe–Ala–OMe (II) (Boc: t-butoxycarbonyl), have been determined by nuclear magnetic resonance (NMR), circular dichroism (CD), and X-ray crystallographic studies. The peptide I assumes a S-shaped flat β-bend structure, characterized by two partially overlapping type II β-bends and absence of a second 1 [LEFTWARDS ARROW] 4 (N4[BOND]H · · · O1′) intramolecular hydrogen bond. This is in contrast to the generally observed 310-helical conformation in peptides with ΔPhe at alternate positions. This report describes the novel conformation assumed by peptide I and compares it with that of the conserved tip of the V3 loop of the HIV-1 envelope glycoprotein gp120 (sequence, G:P319 to F:P324, PDB code 1ACY). The tip of the V3 loop also assumes a S-shaped conformation with Arg:P322, making an intramolecular side-chain–backbone interaction with the carbonyl oxygen of Gly:P319. Interestingly, in peptide I, CγHVal3 makes a similar side-chain–backbone C[BOND]H · · · O hydrogen bond with the carbonyl oxygen of the Boc group. The observed overall similarity indicates the possible use of the peptide as a viral antagonist or synthetic antigen. Peptide II adopts a unique turn followed by a 310-helix. Both peptides I and II are classical examples of stabilization of unusual structures in oligopeptides. © 2006 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 298–309, 2006

This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com