title: Inducing alpha-helices in short oligopeptides through binding by an artificial hydrophobic cavity.
abstract: Short peptides were induced into alpha-helix conformations in water through enclathration to an artificial hydrophobic cavity. Peptides with two aromatic residues showed high affinity for the host, and these intermolecular aromatic-aromatic interactions specifically drove the helical folding of short peptides.
authors.affiliation: Department of Applied Chemistry, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
authors.forename: Christel
authors.initials: C
authors.lastname: Dolain
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Hatakeyama
authors.forename: Tomohisa
authors.initials: T
authors.lastname: Sawada
authors.forename: Shohei
authors.initials: S
authors.lastname: Tashiro
authors.forename: Makoto
authors.initials: M
authors.lastname: Fujita
mesh_terms: D000595:Amino Acid Sequence; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014867:Water / Q000737:chemistry
chemical_list: D009842:Oligopeptides; D014867:Water