Journal Title
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Publisher
Springer, New York, NY
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Authors: Ziqing Jiang Adriana I Vasil John Hale Robert E W Hancock Michael L Vasil Robert S Hodges
Publish Date: 2009
Volume: , Issue: , Pages: 561-562
Abstract
The widespread use of classical antibiotics has resulted in the emergence of many antibioticresistant strains Cationic antimicrobial peptides AMPs have become important candidates as potential therapeutic agents Cationic AMPs of the αhelical class have two unique features a net positive charge of at least +2 and an amphipathic character with a nonpolar face and a polar/charged faceWe previously designed a peptide V13K from our original αhelical antimicrobial peptide V681 which had excellent antimicrobial activity but also exhibited high toxicity 1 DV13K showed greater antimicrobial activity no toxicity and excellent stability to proteolytic digestion compared to DV681 The valine to lysine substitution in the center of the nonpolar face is the first report of a specificity determinant in αhelical antimicrobial peptides between eukaryotic and prokaryotic cells The hydrophobic residues on the nonpolar face of the helix played a more important role in
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