Remodeling of gp41-C34 peptide leads to highly effective inhibitors of the fusion of HIV-1 with target cells

Akira Otaka, Miki Nakamura, Daisuke Nameki, Eiichi Kodama, Susumu Uchiyama, Syota Nakamura, Hiroaki Nakano, Hirokazu Tamamura, Yuji Kobayashi, Masao Matsuoka, Nobutaka Fujii

Research output: Contribution to journalArticle

141 Citations (Scopus)

Abstract

Substitution in the outer surface of the six-helix peptide bundle improved the solubility and enhanced the anti-HIV-1 activity of SC peptides. The E and K residues at positions b, c, f, and g (see scheme) stabilize the a-helix conformation critical to inhibition; the Z residues at positions a, d, and e interact with the inner strand.

Original languageEnglish
Pages (from-to)2937-2940
Number of pages4
JournalAngewandte Chemie - International Edition
Volume41
Issue number16
DOIs
Publication statusPublished - 2002 Aug 16

Keywords

  • Antiviral agents
  • Drug design
  • HIV
  • Helical structures
  • Peptides

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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    Otaka, A., Nakamura, M., Nameki, D., Kodama, E., Uchiyama, S., Nakamura, S., Nakano, H., Tamamura, H., Kobayashi, Y., Matsuoka, M., & Fujii, N. (2002). Remodeling of gp41-C34 peptide leads to highly effective inhibitors of the fusion of HIV-1 with target cells. Angewandte Chemie - International Edition, 41(16), 2937-2940. https://doi.org/10.1002/1521-3773(20020816)41:16<2937::aid-anie2937>3.0.co;2-j