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Stable helical peptoids via covalent side chain to side chain cyclization.

Authors
  • Vaz, Belén
  • Brunsveld, Luc
Type
Published Article
Journal
Organic & Biomolecular Chemistry
Publisher
The Royal Society of Chemistry
Publication Date
Aug 21, 2008
Volume
6
Issue
16
Pages
2988–2994
Identifiers
DOI: 10.1039/b806847j
PMID: 18688493
Source
Medline
License
Unknown

Abstract

Peptoids are oligomeric N-substituted glycines with potential as biologically relevant compounds. Helical peptoids provide an attractive fold for the generation of protein-protein interaction inhibitors. The generation of helical peptoid folds in organic and aqueous media has been limited to strict design rules, as peptoid-folding is mainly directed via the steric direction of alpha-chiral side-chains. Here a new methodology is presented to induce helical folds in peptoids with the aid of side chain to side chain cyclization. Cyclic peptoids were generated via solid-phase synthesis and their folding was studied. The cyclization induces significant helicity in peptoids in organic media, aids the folding in aqueous media, and requires the incorporation of only relatively few chiral aromatic side chains.

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