Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 7, Issue 14, Pages 2872-2877Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b907983a
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- Japan Science and Technology Agency
- MEXT, Japan
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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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