Identification of a β3-peptide HIV fusion inhibitor with improved potency in live cells

被引：30

作者：

Bautista, Arjel D. ^{[1
]}

Stephens, Olen M. ^{[1
]}

Wang, Ligong ^{[3
]}

Domaoal, Robert A. ^{[3
]}

Anderson, Karen S. ^{[3
]}

Schepartz, Alanna ^{[1
,2
]}

机构：

[1] Yale Univ, Dept Chem, New Haven, CT 06520 USA

[2] Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06520 USA

[3] Yale Univ, Sch Med, Dept Pharmacol, New Haven, CT 06510 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2009年 / 19卷 / 14期

关键词：

Foldamer; Peptidomimetic; Anti-viral; Drug design; IMMUNODEFICIENCY-VIRUS TYPE-1; D-PEPTIDE INHIBITORS; BETA-PEPTIDES; IN-VITRO; HTLV-III; ELECTROSTATIC INTERACTIONS; ATOMIC-STRUCTURE; CORE STRUCTURE; COILED-COIL; GP41;

D O I：

10.1016/j.bmcl.2009.05.032

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

We recently reported a beta(3)-decapeptide, beta WWI-1, that binds a validated gp41 model in vitro and inhibits gp41-mediated fusion in cell culture. Here we report six analogs of beta WWI-1 containing a variety of non-natural side chains in place of the central tryptophan of the WWI-epitope. These analogs were compared on the basis of both gp41 affinity in vitro and fusion inibition in live, HIV-infected cells. One new beta(3)-peptide, beta WXI-a, offers a significantly improved CC50/EC50 ratio in the live cell assay. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：3736 / 3738

页数：3

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