Stable helical peptoids via covalent side chain to side chain cyclization.
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.
Vaz
Belén
B
Max Planck Institute of Molecular Physiology, and Chemical Genomics Centre, D-44227, Dortmund, Germany.
Brunsveld
Luc
L
D002942:Circular Dichroism; D003500:Cyclization; D015394:Molecular Structure; D009930:Organic Chemicals / Q000737:chemistry; D034444:Peptoids / Q000138:chemical synthesis* / Q000737:chemistry*; D017433:Protein Structure, Secondary; D014867:Water / Q000737:chemistry
D009930:Organic Chemicals; D034444:Peptoids; D014867:Water