Design of a novel HIV-1 fusion inhibitor that displays a minimal interface for binding affinity

Shinya Oishi, Saori Ito, Hiroki Nishikawa, Kentaro Watanabe, Michinori Tanaka, Hiroaki Ohno, Kazuki Izumi, Yasuko Sakagami, Eiichi Kodama, Masao Matsuoka, Nobutaka Fujii

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

Reported herein are the design, biological activities, and biophysical properties of a novel HIV-1 membrane fusion inhibitor. α-Helix-inducible X-EE-XX-KK motifs were applied to design an enfuvirtide analogue 2 that exhibited highly potent anti-HIV activity against wild-type HIV-1, enfuvirtide-resistant HIV-1 strains, and an HIV-2 strain in vitro. Indispensable residues for bioactivity of enfuvirtide, including the residues interacting with the N-terminal heptad repeat and the C-terminal hydrophobic residues, were identified.

Original languageEnglish
Pages (from-to)388-391
Number of pages4
JournalJournal of Medicinal Chemistry
Volume51
Issue number3
DOIs
Publication statusPublished - 2008 Feb 14
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

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    Oishi, S., Ito, S., Nishikawa, H., Watanabe, K., Tanaka, M., Ohno, H., Izumi, K., Sakagami, Y., Kodama, E., Matsuoka, M., & Fujii, N. (2008). Design of a novel HIV-1 fusion inhibitor that displays a minimal interface for binding affinity. Journal of Medicinal Chemistry, 51(3), 388-391. https://doi.org/10.1021/jm701109d