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 (RhoA77-95). 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.
Original language | English (US) |
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Pages (from-to) | 1-5 |
Number of pages | 5 |
Journal | Current HIV research |
Volume | 9 |
Issue number | 1 |
DOIs | |
State | Published - Feb 22 2011 |
Keywords
- Antiviral
- HIV-1
- Peptides
- RhoA