KMID : 0624620100430050362
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BMB Reports 2010 Volume.43 No. 5 p.362 ~ p.368
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Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles
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Jung Hyun-Ho
Yang Sung-Tae Sim Ji-Yeong Lee Seung-Kyu Lee Ju-Yeon Kim Ha-Hyung Shin Song-Yub Kim Jae-Il
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Abstract
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Dermcidin is a human antibiotic peptide that is secreted by the sweat glands and has no homology to other known antimicrobial peptides. As an initial step toward understanding dermcidin¡¯s mode of action at bacterial membranes, we used homonuclear and heteronuclear NMR to determine the conformation of the peptide in 50% trifluoroethanol solution. We found that dermcidin adopts a flexible amphipathic ¥á-helical structure with a helix-hinge-helix motif, which is a common molecular fold among antimicrobial peptides. Spin-down assays of dermcidin and several related peptides revealed that the affinity with which dermcidin binds to bacterial-mimetic membranes is primarily dependent on its amphipathic ¥á-helical structure and its length (£¾30 residues); its negative net charge and acidic pI have little effect on binding. These findings suggest that the mode of action of dermcidin is similar to that of other membrane-targeting antimicrobial peptides, though the details of its antimicrobial action remain to be determined.
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KEYWORD
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Amphipthic ¥á-helical structure, Antimicrobial peptide, Helix-hinge-helix motif, Nuclear magnetic resonance (NMR) spectroscopy, Peptide-membrane interaction
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