title: Conformational rearrangements by water-soluble peptoid foldamers.
abstract: Peptoids are a family of N-substituted glycine oligomers that are capable of forming stable helical structures. We seek peptoid monomers that can establish a strong folding propensity in aqueous conditions. Here we utilize L-phenylalanine tert-butyl ester as a readily available reagent for the synthesis of (S)-N-(1-carboxy-2-phenylethyl)glycine oligomers. The products form stable secondary structures in aqueous solution in which the conformation is dramatically responsive to variations in pH and solvent composition.
authors.affiliation: Department of Chemistry, New York University, 100 Washington Square East, New York, New York 10003-6688, USA.
authors.forename: Sung Bin Y
authors.initials: SB
authors.lastname: Shin
authors.forename: Kent
authors.initials: K
authors.lastname: Kirshenbaum
mesh_terms: D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D034444:Peptoids / Q000138:chemical synthesis* / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012995:Solubility; D014867:Water / Q000737:chemistry
chemical_list: D034444:Peptoids; D014867:Water