title: Solution structure of antimicrobial peptide esculentin-1c from skin secretion of Rana esculenta.
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.
authors.affiliation: Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, 151-742, Korea.
authors.forename: Su-Jin
authors.initials: SJ
authors.lastname: Kang
authors.forename: Woo-Sung
authors.initials: WS
authors.lastname: Son
authors.forename: Kyung-Doo
authors.initials: KD
authors.lastname: Han
authors.forename: Tsogbadrakh
authors.initials: T
authors.lastname: Mishig-Ochir
authors.forename: Dae-Woo
authors.initials: DW
authors.lastname: Kim
authors.forename: Jae-Il
authors.initials: JI
authors.lastname: Kim
authors.forename: Bong-Jin
authors.initials: BJ
authors.lastname: Lee
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000378:metabolism; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D011893:Rana esculenta / Q000378:metabolism*; D020539:Sequence Analysis, Protein; D012867:Skin / Q000737:chemistry / Q000378:metabolism*; D012996:Solutions
chemical_list: D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D012996:Solutions; C092874:esculentin protein, Rana esculenta; C077195:helical erythrocyte lysing peptide