Peptide bond mimicry by (E)-alkene and (Z)-fluoroalkene peptide isosteres: synthesis and bioevaluation of α-helical anti-HIV peptide analogues
Organic & Biomolecular Chemistry2009Vol. 7(14), pp. 2872–2872
Citations Over TimeTop 17% of 2009 papers
Shinya Oishi, Hirotaka Kamitani, Yasuyo Kodera, Kentaro Watanabe, Kazuya Kobayashi, Tetsuo Narumi, Kenji Tomita, Hiroaki Ohno, Takeshi Naito, Eiichi Kodama, Masao Matsuoka, Nobutaka Fujii
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.
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