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2000
Volume 9, Issue 1
  • ISSN: 1570-162X
  • E-ISSN: 1873-4251

Abstract

RhoA-derived peptides have been shown to have antiviral activity against both human respiratory syncytial virus and human parainfluenza virus-3. The present study investigates the toxicity, anti-HIV-1 activity and mechanism of action of a RhoA-derived peptide (RhoA 77-95). The efficacy of this peptide was compared to a scrambled peptide of the same amino acid composition and Enfuvirtide, a HIV entry inhibitor. Our data show that this RhoA-derived peptide is a non-toxic and effective inhibitor of a CXCR4 tropic strain of HIV-1. We also demonstrate that the mechanism of entry inhibition is likely mediated by polyanionic properties and is dependent on the dimerization of peptides.

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/content/journals/chr/10.2174/157016211794582605
2011-01-01
2025-09-04
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/content/journals/chr/10.2174/157016211794582605
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  • Article Type:
    Research Article
Keyword(s): Antiviral; HIV-1; Peptides; RhoA
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