Journal
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
Volume 52, Issue 6, Pages 2120-2129Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.01424-07
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Funding
- NEI NIH HHS [EY016665, EY07336, R01 EY007336, P30 EY016665] Funding Source: Medline
- NIAID NIH HHS [P01 AI052049, AI52089] Funding Source: Medline
- NIGMS NIH HHS [GM56414, T32GM008505, R01 GM056414, T32 GM008505] Funding Source: Medline
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Previously, it was shown that cationic alpha-peptides derived from the human immunodeficiency virus TAT protein transduction domain blocked herpes simplex virus type 1 (HSV-1) entry. We now show that cationic oligomers of beta-amino acids (beta-peptides) inhibit HSV-1 infection. Among three cationic beta-peptides tested, the most effective inhibition was observed for the one with a strong propensity to adopt a helical conformation in which cationic and hydrophobic residues are segregated from one another (globally amphiphilic helix). The antiviral effect was not cell type specific. Inhibition of virus infection by the beta-peptides occurred at the postattachment penetration step, with a 50% effective concentration of 3 mu M for the most-effective beta-peptide. The beta-peptides did not inactivate virions in solution, nor did they induce resistance to infection when cells were pretreated with the beta-peptides. The beta-peptides showed little if any toxicity toward Vero cells. These results raise the possibility that cationic beta-peptides may be useful antiviral agents for HSV-1 and demonstrate the potential of beta-peptides as novel antiviral drugs.
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