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KMID : 0578320100300050435
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Molecules and Cells
2010 Volume.30 No. 5 p.435 ~ p.441
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Solution Structure of Antimicrobial Peptide Esculentin-1c from Skin Secretion of Rana esculenta
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Kang Su-Jin
Son Woo-Sung
Han Kyung-Doo
Tsogbadrakh Mishig-Ochir
Kim Dae-Woo
Kim Jae-Il
Lee Bong-Jin
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Abstract
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Granular glands in the skins of frogs synthesize and secrete a remarkably diverse range of peptides capable of antimicrobial activity. These anuran skin antimicrobial peptides are commonly hydrophobic, cationic and form an amphipathic α-helix in a membrane mimetic solution. Recently, they have been considered as useful target molecules for developing new antibiotics drugs. Esculentin-1c is a 46-amino acid residue peptide isolated from skin secretions of the European frog, Rana esculenta. It displays the most potent antimicrobial activity among bioactive molecules. Esculentin-1c has the longest amino acids among all antimicrobial peptides. The present study solved the solution structure of esculentin-1c in TFE/water by NMR, for the first time. We conclude that this peptide is comprised of three α-helices with each helix showing amphipathic characteristics, which seems to be a key part for permeating into bacterial membranes, thus presenting antimicrobial activity.
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KEYWORD
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antimicrobial peptide, nuclear magnetic resonance, solution structure
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