title: Peptide bond mimicry by (E)-alkene and (Z)-fluoroalkene peptide isosteres: synthesis and bioevaluation of alpha-helical anti-HIV peptide analogues.
abstract: The alpha-helix structures of the anti-HIV fusion inhibitory peptides are stabilized by the amino acid sequence and by intrachain hydrogen bonds. The study of peptide analogues using (E)-alkene and (Z)-fluoroalkene dipeptide isosteres demonstrated the substantial, yet position-dependent, contribution of hydrogen bonds to the alpha-helix stability and anti-HIV bioactivity.
authors: Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan. soishi@pharm.kyoto-u.ac.jp
authors: Shinya
authors: S
authors: Oishi
authors: Hirotaka
authors: H
authors: Kamitani
authors: Yasuyo
authors: Y
authors: Kodera
authors: Kentaro
authors: K
authors: Watanabe
authors: Kazuya
authors: K
authors: Kobayashi
authors: Tetsuo
authors: T
authors: Narumi
authors: Kenji
authors: K
authors: Tomita
authors: Hiroaki
authors: H
authors: Ohno
authors: Takeshi
authors: T
authors: Naito
authors: Eiichi
authors: E
authors: Kodama
authors: Masao
authors: M
authors: Matsuoka
authors: Nobutaka
authors: N
authors: Fujii
mesh_terms: D000475:Alkenes / Q000737:chemistry*; D000595:Amino Acid Sequence; D019380:Anti-HIV Agents / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D032701:Biomimetics; D005461:Fluorine / Q000737:chemistry*; D006678:HIV / Q000187:drug effects*; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D017433:Protein Structure, Secondary; D013237:Stereoisomerism
chemical_list: D000475:Alkenes; D019380:Anti-HIV Agents; D010455:Peptides; D005461:Fluorine