Journal
JOURNAL OF PEPTIDE SCIENCE
Volume 13, Issue 7, Pages 481-486Publisher
WILEY
DOI: 10.1002/psc.876
Keywords
cationic Aib-containing peptides; antimicrobial activity; proteolytic stability; hemolytic assay; circular dichroism
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Development of antimicrobial peptides has attracted considerable attention in recent years due to the excessive use of antibiotics, which has led to multiresislant bacteria. Cationic amphiphilic Alb-containing peptide models Ac-(Aib-ArgAib-Leu)(n)-NH2, n = 1-4, and sequential cationic polypeptides (Arg-X-Gly)(n), X = Ala, Val, Leu, were prepared and studied for their antimicrobial and hemolytic activity, as well as for their proteolytic stability. Ac-(Aib-Arg-Aib-Leu)(n)-NH2, n = 2, 3 and the polypeptide (Arg-Leu-Gly)(n) exhibited significant antimicrobial activity, and they were nontoxic at their MIC values and resistant, in particular the Aib-peptide models, to enzymatic degradation. The conformational characteristics of the peptide models were studied by circular dichroism (CD). Structure-activity relationship studies revealed the importance of the amphipathic a-helical conformation of the reported peptides in inducing antimicrobial effects. It is concluded that peptide models comprising cationic amino acids (Arg), helicogenic and noncoding residues (Aib) and/or hydrophobic and helix-promoting components (Leu) may lead to the development of antimicrobial therapeutics. Copyright (C) 2007 European Peptide Society and John Wiley & Sons, Ltd.
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