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

doi:10.1002/1521-3773(20020816)41:16<2937::aid-anie2937>3.0.co;2-j

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

IRIDeS - Disaster Medical Science Division

Research output: Contribution to journal › Article › peer-review

156 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 language	English
Pages (from-to)	2937-2940
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	41
Issue number	16
DOIs	https://doi.org/10.1002/1521-3773(20020816)41:16<2937::aid-anie2937>3.0.co;2-j
Publication status	Published - 2002 Aug 16

Keywords

Antiviral agents
Drug design
Helical structures
HIV
Peptides

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/1521-3773(20020816)41:16<2937::aid-anie2937>3.0.co;2-j

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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

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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.",

keywords = "Antiviral agents, Drug design, Helical structures, HIV, Peptides",

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

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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, vol. 41, no. 16, pp. 2937-2940. https://doi.org/10.1002/1521-3773(20020816)41:16<2937::aid-anie2937>3.0.co;2-j

TY - JOUR

T1 - Remodeling of gp41-C34 peptide leads to highly effective inhibitors of the fusion of HIV-1 with target cells

AU - Otaka, Akira

AU - Nakamura, Miki

AU - Nameki, Daisuke

AU - Kodama, Eiichi

AU - Uchiyama, Susumu

AU - Nakamura, Syota

AU - Nakano, Hiroaki

AU - Tamamura, Hirokazu

AU - Kobayashi, Yuji

AU - Matsuoka, Masao

AU - Fujii, Nobutaka

PY - 2002/8/16

Y1 - 2002/8/16

N2 - 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.

AB - 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.

KW - Antiviral agents

KW - Drug design

KW - Helical structures

KW - HIV

KW - Peptides

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U2 - 10.1002/1521-3773(20020816)41:16<2937::aid-anie2937>3.0.co;2-j

DO - 10.1002/1521-3773(20020816)41:16<2937::aid-anie2937>3.0.co;2-j

M3 - Article

C2 - 12203417

AN - SCOPUS:0037119022

SN - 1433-7851

VL - 41

SP - 2937

EP - 2940

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 16

ER -

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

Abstract

Keywords

UN SDGs

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