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

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59 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2872-2877
Number of pages6
JournalOrganic and Biomolecular Chemistry
Volume7
Issue number14
DOIs
Publication statusPublished - 2009 Jul 20
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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    Oishi, S., Kamitani, H., Kodera, Y., Watanabe, K., Kobayashi, K., Narumi, T., Tomita, K., Ohno, H., Naito, T., Kodama, E., Matsuoka, M., & Fujii, N. (2009). Peptide bond mimicry by (E)-alkene and (Z)-fluoroalkene peptide isosteres: Synthesis and bioevaluation of α-helical anti-HIV peptide analogues. Organic and Biomolecular Chemistry, 7(14), 2872-2877. https://doi.org/10.1039/b907983a