title: Introduction of cyclically constrained γ-residues stabilizes an α-peptide hairpin in aqueous solution.
abstract: The synthesis and structural characterization of hybrid α/γ-peptides resulting from a 1:1 α→γ residue substitution at cross-strand positions in a hairpin-forming α-peptide sequence are described. Cyclically constrained γ-residues based on 1,3-substituted cyclohexane or benzene scaffolds support a native-like hairpin fold in aqueous solution, and the unnatural residues stabilize the folded state by ∼0.2 kcal/mol per α→γ substitution.
authors: Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States.
authors: George A
authors: GA
authors: Lengyel
authors: Geoffrey A
authors: GA
authors: Eddinger
authors: W Seth
authors: WS
authors: Horne
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D003510:Cyclohexanes / Q000737:chemistry*; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D000596:Amino Acids; D003510:Cyclohexanes; D010455:Peptides; D012996:Solutions; D014867:Water