Design of antiviral stapled peptides containing a biphenyl cross-linker.
Bioorg Med Chem Lett
; 24(7): 1748-51, 2014 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-24613163
ABSTRACT
Here we report the design and synthesis of a panel of stapled peptides containing a distance-matching biphenyl cross-linker based upon a peptide capsid assembly inhibitor reported previously. Compared with the linear peptide, the biphenyl-stapled peptides exhibited significantly enhanced cell penetration and potent antiviral activity in the cell-based infection assays. Isothermal titration calorimetry and surface plasmon resonance experiments revealed that the most active stapled CAI peptide binds to the C-terminal domain of HIV capsid protein as well as envelop glycoprotein gp120 with low micromolar binding affinities, and as a result, inhibits both the HIV-1 virus entry and the virus assembly.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
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Compostos de Bifenilo
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Desenho de Fármacos
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HIV-1
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Fármacos Anti-HIV
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Reagentes de Ligações Cruzadas
Limite:
Humans
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article