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 Hong, S. Y.
Right arrow Articles by Lee, K. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hong, S. Y.
Right arrow Articles by Lee, K. H.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, October 1998, p. 2534-2541, Vol. 42, No. 10
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Identification and Characterization of Novel Antimicrobial Decapeptides Generated by Combinatorial Chemistry

Sung Yu Hong,1 Jong Eun Oh,1 Mi yun Kwon,1 Myeong Jun Choi,1 Ji Hye Lee,2 Bok Luel Lee,2 Hong Mo Moon,1 and Keun Hyeung Lee1,*

Protein Chemistry Laboratory, Mogam Biotechnology Research Institute, Kyunggi-Do, 449-910,1 and College of Pharmacy, Pusan National University, Pusan 609-735,2 Korea

Received 28 January 1998/Returned for modification 8 June 1998/Accepted 15 July 1998

Novel combinatorial libraries consisting of simplified amino acid sequences were designed to screen for peptides active against the Candida albicans membrane. A novel decapeptide, KKVVFKVKFK, that had a unique primary amino acid sequence was identified in this work. This peptide irreversibly inhibited the growth of C. albicans and showed a broad range of antibacterial activity but no hemolytic activity. Circular dichroism spectra revealed that the predominant secondary structure of this peptide strongly depended on the membrane-mimetic environments; the peptide preferred to form an amphipathic alpha -helical structure in the presence of 50% trifluoroethanol, while it preferred to adopt a distorted alpha -helical structure in the presence of sodium dodecyl sulfate micelles. Experiments in which dye was released from vesicles indicated that this novel antimicrobial peptide killed microorganisms through the action on the membrane as its primary target. Replacement of amino acids in this active decapeptide on the basis of information from the libraries could provide unique information about factors affecting its antimicrobial activity such as its secondary structure, net positive charge, and hydrophobicity.

* Corresponding author. Mailing address: Protein Chemistry Laboratory, Mogam Biotechnology Research Institute, 341 Pojung-Ri, Koosung-Myun, Yongin City, Kyonggi-Do, 449-910, Korea. Phone: 82-331-262-3851. Fax: 82-331-262-6622. E-mail: lkh{at}kgcc.co.kr.

Antimicrobial Agents and Chemotherapy, October 1998, p. 2534-2541, Vol. 42, No. 10
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Yadav, V., Mandhan, R., Pasha, Q., Pasha, S., Katyal, A., Chhillar, A. K., Gupta, J., Dabur, R., Sharma, G. L. (2007). An antifungal protein from Escherichia coli. J Med Microbiol 56: 637-644 [Abstract] [Full Text]  
  • Niimi, K., Harding, D. R. K., Parshot, R., King, A., Lun, D. J., Decottignies, A., Niimi, M., Lin, S., Cannon, R. D., Goffeau, A., Monk, B. C. (2004). Chemosensitization of Fluconazole Resistance in Saccharomyces cerevisiae and Pathogenic Fungi by a D-Octapeptide Derivative. Antimicrob. Agents Chemother. 48: 1256-1271 [Abstract] [Full Text]  
  • Concannon, S. P., Crowe, T. D., Abercrombie, J. J., Molina, C. M., Hou, P., Sukumaran, D. K., Raj, P. A., Leung, K. -P. (2003). Susceptibility of oral bacteria to an antimicrobial decapeptide. J Med Microbiol 52: 1083-1093 [Abstract] [Full Text]  
  • Lopez-Garcia, B., Perez-Paya, E., Marcos, J. F. (2002). Identification of Novel Hexapeptides Bioactive against Phytopathogenic Fungi through Screening of a Synthetic Peptide Combinatorial Library. Appl. Environ. Microbiol. 68: 2453-2460 [Abstract] [Full Text]  
  • TAN, N. S., NG, M. L. P., YAU, Y. H., CHONG, P. K. W., HO, B., DING, J. L. (2000). Definition of endotoxin binding sites in horseshoe crab Factor C recombinant sushi proteins and neutralization of endotoxin by sushi peptides. FASEB J. 14: 1801-1813 [Abstract] [Full Text]  
  • Andriole, V. T. (1999). Current and future antifungal therapy: new targets for antifungal agents. J Antimicrob Chemother 44: 151-162 [Abstract] [Full Text]  
  • Hong, S. Y., Oh, J. E., Lee, K. H. (1999). In Vitro Antifungal Activity and Cytotoxicity of a Novel Membrane-Active Peptide. Antimicrob. Agents Chemother. 43: 1704-1707 [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»