Stapled peptide-based membrane fusion inhibitors of hepatitis C virus.
| Autor: | Cui HK; Tsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China., Qing J, Guo Y, Wang YJ, Cui LJ, He TH, Zhang L, Liu L |
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| Jazyk: | angličtina |
| Zdroj: | Bioorganic & medicinal chemistry [Bioorg Med Chem] 2013 Jun 15; Vol. 21 (12), pp. 3547-54. Date of Electronic Publication: 2013 Feb 21. |
| DOI: | 10.1016/j.bmc.2013.02.011 |
| Abstrakt: | 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 α-helicity and proteolytic stability as compared to their linear peptide counterpart. The optimal compound was found to have an EC50 value of ca. 17-39μM against different HCV subtypes and represented a new HCV membrane fusion inhibitor. (Copyright © 2013 Elsevier Ltd. All rights reserved.) |
| Databáze: | MEDLINE |
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