This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Akkarawongsa, R.
Right arrow Articles by Brandt, C. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Akkarawongsa, R.
Right arrow Articles by Brandt, C. R.

 Previous Article  |  Next Article 

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{triangledown}

Radeekorn Akkarawongsa,1 Terra B. Potocky,2,{dagger} Emily P. English,2 Samuel H. Gellman,2 and Curtis R. Brandt1,3,4*

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 {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 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.


* Corresponding author. Mailing address: Department of Ophthalmology and Visual Sciences, University of Wisconsin School of Medicine and Public Health, 6630 Medical Sciences Center, 1300 University Avenue, Madison, WI 53706. Phone: (608) 262-8054. Fax: (608) 262-0479. E-mail: crbrandt{at}wisc.edu

{triangledown} Published ahead of print on 7 April 2008.

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


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.