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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
Sep 30, 2023 Vol.46 No.9, pp. 527~572
COVER PICTURE
Chronic obstructive pulmonary disease (COPD) is marked by airspace enlargement (emphysema) and small airway fibrosis, leading to airflow obstruction and eventual respiratory failure. Shown is a microphotograph of hematoxylin and eosin (H&E)-stained histological sections of the enlarged alveoli as an indicator of emphysema. Piao et al. (pp. 558-572) demonstrate that recombinant human hyaluronan and proteoglycan link protein 1 (rhHAPLN1) significantly reduces the extended airspaces of the emphysematous alveoli by increasing the levels of TGF-β receptor I and SIRT1/6, as a previously unrecognized mechanism in human alveolar epithelial cells, and consequently mitigates COPD.

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