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Bioorg Med Chem ; 21(12): 3547-54, 2013 Jun 15.
Artigo em Inglês | MEDLINE | ID: mdl-23490158

RESUMO

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.


Assuntos
Hepacivirus/efeitos dos fármacos , Hepatite C/tratamento farmacológico , Peptídeos/química , Relação Dose-Resposta a Droga , Humanos , Testes de Sensibilidade Microbiana , Modelos Moleculares , Estrutura Molecular , Peptídeos/síntese química , Relação Estrutura-Atividade
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