Peptide bond mimicry by (E)-alkene and (Z)-fluoroalkene peptide isosteres: synthesis and bioevaluation of α-helical anti-HIV peptide analogues

Shinya Oishi; Hirotaka Kamitani; Yasuyo Kodera; Kentaro Watanabe; Kazuya Kobayashi; Tetsuo Narumi; Kenji Tomita; Hiroaki Ohno; Takeshi Naito; Eiichi Kodama; Masao Matsuoka; Nobutaka Fujii

doi:10.1039/B907983A

Peptide bond mimicry by (E)-alkene and (Z)-fluoroalkene peptide isosteres: synthesis and bioevaluation of α-helical anti-HIV peptide analogues†

Shinya Oishi,*^a Hirotaka Kamitani,^a Yasuyo Kodera,^a Kentaro Watanabe,^a Kazuya Kobayashi,^a Tetsuo Narumi,^a Kenji Tomita,^a Hiroaki Ohno,^a Takeshi Naito,^b Eiichi Kodama,^b Masao Matsuoka^b and Nobutaka Fujii*^a

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^a Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan
E-mail: soishi@pharm.kyoto-u.ac.jp, nfujii@pharm.kyoto-u.ac.jp
Fax: +81-75-753-4570
Tel: +81-75-753-4551

^b Laboratory of Virus Control, Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto, Japan

Abstract

The α-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 α-helix stability and anti-HIV bioactivity.

Organic & Biomolecular Chemistry

Peptide bond mimicry by (E)-alkene and (Z)-fluoroalkene peptide isosteres: synthesis and bioevaluation of α-helical anti-HIV peptide analogues†

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Peptide bond mimicry by (E)-alkene and (Z)-fluoroalkene peptide isosteres: synthesis and bioevaluation of α-helical anti-HIV peptide analogues

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