Stable helical peptoids via covalent side chain to side chain cyclization

B. Vaz, L. Brunsveld

Research output: Contribution to journalArticleAcademicpeer-review

26 Citations (Scopus)
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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.
Original languageEnglish
Pages (from-to)2988-2994
Number of pages7
JournalOrganic & Biomolecular Chemistry
Publication statusPublished - 2008


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