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A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus
Author(s) -
Park Chan Bae,
Lee Jae Hyun,
Park In Yup,
Kim Mi Sun,
Kim Sun Chang
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00684-4
Subject(s) - magainin , peptide , edman degradation , misgurnus , peptide sequence , antimicrobial peptides , antimicrobial , biochemistry , amino acid , chemistry , biology , microbiology and biotechnology , fishery , fish <actinopterygii> , gene
A novel antimicrobial peptide, named misgurin, was isolated and characterized from the loach (mudfish), Misgurnus anguillicaudatus . The 21‐amino‐acid peptide with a molecular mass of 2502 Da was purified to homogeneity using a heparin‐affinity column and C18 reverse‐phase and gel‐permeation high‐performance liquid chromatography. The complete amino acid sequence of misgurin, which was determined by an automated amino acid sequencer, was Arg–Gln–Arg–Val–Glu–Glu–Leu–Ser–Lys–Phe–Ser–Lys–Lys–Gly–Ala–Ala–Ala–Arg–Arg–Arg–Lys. Misgurin is a strongly basic peptide which has 5 arginine and 4 lysine residues. Comparison of the amino acid sequence with those of other known antimicrobial peptides revealed that misgurin was a novel antimicrobial peptide. Misgurin showed a strong antimicrobial activity in vitro against a broad spectrum of microorganisms without significant hemolytic activity and was about 6 times more potent than magainin 2. Scanning electron microscopy confirmed that the peptide caused damage to the cell membrane by a pore‐forming mechanism similar to that of magainin 2. This damage occurred at the minimal inhibition concentration (MIC), but at higher concentration than MIC it lysed the cell.