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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wang, G.
Right arrow Articles by Buckheit, R. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wang, G.
Right arrow Articles by Buckheit, R. W., Jr.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, September 2008, p. 3438-3440, Vol. 52, No. 9
0066-4804/08/$08.00+0     doi:10.1128/AAC.00452-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Anti-Human Immunodeficiency Virus Type 1 Activities of Antimicrobial Peptides Derived from Human and Bovine Cathelicidins {triangledown}

Guangshun Wang,1* Karen M. Watson,2 and Robert W. Buckheit Jr.2

The Structure-Fun Laboratory, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, 986805 Nebraska Medical Center, Omaha, Nebraska 68198,1 ImQuest BioSciences, Inc., 7340 Executive Way, Suite R, Frederick, Maryland 217042

Received 4 April 2008/ Returned for modification 23 May 2008/ Accepted 20 June 2008

From among 15 human cathelicidin LL-37-derived peptides, FK-13 was identified as the smallest peptide active against human immunodeficiency virus (HIV) and GI-20 had the highest therapeutic index, which was twice that of LL-37. BMAP-18, which is derived from bovine cathelicidin BMAP-27, possessed a therapeutic index similar to that of GI-20. Peptide sequence order, helical structures, and aromatic residues are important in HIV inhibition.

* Corresponding author. Mailing address: Eppley Cancer Institute, Room ECI 3018, University of Nebraska Medical Center, 986805 Nebraska Medical Center, Omaha, NE 68198-6805. Phone: (402) 559-4176. Fax: (402) 559-4651. E-mail: gwang{at}unmc.edu

{triangledown} Published ahead of print on 30 June 2008.

Antimicrobial Agents and Chemotherapy, September 2008, p. 3438-3440, Vol. 52, No. 9
0066-4804/08/$08.00+0     doi:10.1128/AAC.00452-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chakraborty, K., Maity, P. C., Sil, A. K., Takeda, Y., Das, S. (2009). cAMP Stringently Regulates Human Cathelicidin Antimicrobial Peptide Expression in the Mucosal Epithelial Cells by Activating cAMP-response Element-binding Protein, AP-1, and Inducible cAMP Early Repressor. J. Biol. Chem. 284: 21810-21827 [Abstract] [Full Text]  
  • Wang, G., Li, X., Wang, Z. (2009). APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res 37: D933-D937 [Abstract] [Full Text]  
  • Wang, G. (2008). Structures of Human Host Defense Cathelicidin LL-37 and Its Smallest Antimicrobial Peptide KR-12 in Lipid Micelles. J. Biol. Chem. 283: 32637-32643 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»