Stapled peptide-based membrane fusion inhibitors of hepatitis C virus
Stapled peptide-based membrane fusion inhibitors of hepatitis C virus
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基于钉合肽的丙型肝炎病毒膜融合抑制剂。
DOI：
10.1016/j.bmc.2013.02.011
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发表时间：
2013-06-15
影响因子：
3.5
通讯作者：
Liu, Lei
中科院分区：
文献类型：
--
作者：
Cui, Hong-Kui;Qing, Jie;Liu, Lei
利用肽钉合的策略，通过破坏HCV包膜糖蛋白E2与人细胞表面蛋白CD 81的结合来开发新的抑制丙型肝炎病毒感染的分子。肽序列是基于已知在HCV E2结合相互作用中具有重要性的CD 81的大细胞外环设计的。我们的结果表明，与线性肽对应物相比，钉合肽表现出显著更高的α-螺旋度和蛋白水解稳定性。发现最佳化合物的EC 50值为约1.5。17-39 μ M，代表一种新的HCV膜融合抑制剂。(C)2013爱思唯尔有限公司保留所有权利。
The strategy of peptide stapling was used to develop new molecules to inhibit the hepatitis C virus infection via disrupting the binding of HCV envelope glycoprotein E2 with human cell surface protein CD81. The peptide sequence was designed based on the large extra-cellular loop of CD81 with known importance in the HCV E2 binding interaction. Our results showed that the stapled peptides exhibited significantly higher alpha-helicity and proteolytic stability as compared to their linear peptide counterpart. The optimal compound was found to have an EC50 value of ca. 17-39 mu M against different HCV subtypes and represented a new HCV membrane fusion inhibitor. (C) 2013 Elsevier Ltd. All rights reserved.