Mol. Cells 2010; 30(5): 435-441
Published online September 10, 2010
https://doi.org/10.1007/s10059-010-0135-7
© The Korean Society for Molecular and Cellular Biology
Correspondence to : *Correspondence: lbj@nmr.snu.ac.kr
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.
Keywords antimicrobial peptide, nuclear magnetic resonance, solution structure
Mol. Cells 2010; 30(5): 435-441
Published online November 30, 2010 https://doi.org/10.1007/s10059-010-0135-7
Copyright © The Korean Society for Molecular and Cellular Biology.
Su-Jin Kang, Woo-Sung Son, Kyung-Doo Han, Tsogbadrakh Mishig-Ochir1, Dae-Woo Kim2, Jae-Il Kim2, and Bong-Jin Lee*
Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, Korea, 1Department of Biophysics, Faculty of Biology, National University of Mongolia, Ulaanbaatar, Mongolia, 2Department of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea
Correspondence to:*Correspondence: lbj@nmr.snu.ac.kr
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.
Keywords: antimicrobial peptide, nuclear magnetic resonance, solution structure
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