TOP

Research Article

Split Viewer

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

Solution Structure of Antimicrobial Peptide Esculentin-1c from Skin Secretion of Rana esculenta

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

Received: May 10, 2010; Revised: August 13, 2010; Accepted: August 16, 2010

Abstract

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

Article

Research Article

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.

Solution Structure of Antimicrobial Peptide Esculentin-1c from Skin Secretion of Rana esculenta

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

Received: May 10, 2010; Revised: August 13, 2010; Accepted: August 16, 2010

Abstract

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
May 31, 2023 Vol.46 No.5, pp. 259~328
COVER PICTURE
The alpha-helices in the lamin filaments are depicted as coils, with different subdomains distinguished by various colors. Coil 1a is represented by magenta, coil 1b by yellow, L2 by green, coil 2a by white, coil 2b by brown, stutter by cyan, coil 2c by dark blue, and the lamin Ig-like domain by grey. In the background, cells are displayed, with the cytosol depicted in green and the nucleus in blue (Ahn et al., pp. 309-318).

Share this article on

  • line
  • mail

Related articles in Mol. Cells

Molecules and Cells

eISSN 0219-1032
qr-code Download