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Antimicrobial Agents and Chemotherapy, June 2008, p. 2120-2129, Vol. 52, No. 6
0066-4804/08/$08.00+0     doi:10.1128/AAC.01424-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Inhibition of Herpes Simplex Virus Type 1 Infection by Cationic β-Peptides

Radeekorn Akkarawongsa,¹ Terra B. Potocky,^2, Emily P. English,² Samuel H. Gellman,² and Curtis R. Brandt^1,3,4*

Program in Cell and Molecular Biology,¹ Department of Chemistry,² Department of Medical Microbiology and Immunology,³ Department of Ophthalmology and Visual Sciences, University of Wisconsin—Madison, Madison, Wisconsin 53706⁴

Received 2 November 2007/ Returned for modification 17 December 2007/ Accepted 28 March 2008

Previously, it was shown that cationic -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 β-amino acids ("β-peptides") inhibit HSV-1 infection. Among three cationic β-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 β-peptides occurred at the postattachment penetration step, with a 50% effective concentration of 3 µM for the most-effective β-peptide. The β-peptides did not inactivate virions in solution, nor did they induce resistance to infection when cells were pretreated with the β-peptides. The β-peptides showed little if any toxicity toward Vero cells. These results raise the possibility that cationic β-peptides may be useful antiviral agents for HSV-1 and demonstrate the potential of β-peptides as novel antiviral drugs.

Published ahead of print on 7 April 2008.

Present address: Department of Biology, Higgins Hall, Room 410, Boston College, 140 Commonwealth Ave., Chestnut Hill, MA 02467.