title: Stabilization of β-peptide helices by direct attachment of trifluoromethyl groups to peptide backbones.
abstract: The 14-helix structure of oligo-β-peptides was significantly stabilized by direct attachment of CF3 groups to their backbones. Our studies indicate that this stabilization originates from the CF3-promoted increase in the intramolecular hydrogen-bonding ability of their backbone amides, leading to a novel strategy to stabilize peptide folding.
authors.affiliation: RIKEN Center for Emergent Matter Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. y-ishida@riken.jp.
authors.forename: Joonil
authors.initials: J
authors.lastname: Cho
authors.forename: Kyohei
authors.initials: K
authors.lastname: Sawaki
authors.forename: Shinya
authors.initials: S
authors.lastname: Hanashima
authors.forename: Yoshiki
authors.initials: Y
authors.lastname: Yamaguchi
authors.forename: Motoo
authors.initials: M
authors.lastname: Shiro
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Saigo
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Ishida
mesh_terms: D000577:Amides / Q000737:chemistry; D018360:Crystallography, X-Ray; D054879:Halogenation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary
chemical_list: D000577:Amides; D010455:Peptides