Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 6, Issue 16, Pages 2988-2994Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b806847j
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Funding
- Alexander von Humboldt Foundation
- BNIBF
- Spanish Ministerio de Educacion y Ciencia
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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 a-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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