Design of a novel HIV-1 fusion inhibitor that displays a minimal interface for binding affinity.
Design of a novel HIV-1 fusion inhibitor that displays a minimal interface for binding affinity.
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DOI：
10.1021/jm701109d
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发表时间：
2008-01
影响因子：
7.3
通讯作者：
S. Oishi;Saori Ito;Hiroki Nishikawa;Kentaro Watanabe;Michinori Tanaka;H. Ohno;Kazuki Izumi;
中科院分区：
文献类型：
--
作者：
S. Oishi;Saori Ito;Hiroki Nishikawa;Kentaro Watanabe;Michinori Tanaka;H. Ohno;Kazuki Izumi;
本文报道了一种新型HIV-1膜融合抑制剂的设计、生物活性和生物物理性质。应用α-受阻素诱导的X-EE-XX-KK基序设计恩夫韦肽类似物2，其在体外对野生型HIV-1、恩夫韦肽抗性HIV-1株和HIV-2株表现出高度有效的抗HIV活性。鉴定了恩夫韦肽生物活性的抑制残基，包括与N-末端七肽重复序列相互作用的残基和C-末端疏水残基。
Reported herein are the design, biological activities, and biophysical properties of a novel HIV-1 membrane fusion inhibitor. alpha-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.