Identification and Characterization of Novel Antimicrobial Decapeptides Generated by Combinatorial Chemistry
AUTOR(ES)
Hong, Sung Yu
FONTE
American Society for Microbiology
RESUMO
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 α-helical structure in the presence of 50% trifluoroethanol, while it preferred to adopt a distorted α-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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=105883Documentos Relacionados
- Synthetic combinatorial libraries: novel discovery strategy for identification of antimicrobial agents.
- Novel folded protein domains generated by combinatorial shuffling of polypeptide segments
- Identification of antimicrobial peptides by using combinatorial libraries made up of unnatural amino acids.
- Encoded combinatorial chemistry.
- Combinatorial thinking in chemistry and biology