A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus
A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus
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DOI：
10.1016/s0014-5793(97)00684-4
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发表时间：
1997-07
期刊：
影响因子：
3.5
通讯作者：
C. Park;Jae Hyun Lee;I. Park;Mi Sun Kim;S. C. Kim
中科院分区：
文献类型：
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作者：
C. Park;Jae Hyun Lee;I. Park;Mi Sun Kim;S. C. Kim
从泥鳅（Misgurnus anguillicaudatus）中分离得到一种新的抗菌肽，命名为Misgurin。使用肝素亲和柱和C18反相和凝胶渗透高效液相色谱法将分子量为2502 Da的21-氨基酸肽纯化至均一。通过氨基酸自动测序仪测定，其氨基酸序列为Arg-Gln-Arg-Val-Glu-Glu-Leu-Ser-Lys-Phe-Ser-Lys-Lys-Gly-Ala-Ala-Ala-Arg-Arg-Arg-Lys。Misgurin是一种强碱性肽，具有5个精氨酸和4个赖氨酸残基。氨基酸序列与已知的抗菌肽序列比较表明，泥鳅蛋白是一种新的抗菌肽。Misgurin在体外对广谱微生物显示出强的抗微生物活性，而没有显著的溶血活性，并且比爪蟾抗菌肽2强约6倍。扫描电子显微镜证实，该肽通过类似于爪蟾抗菌肽2的成孔机制对细胞膜造成损伤。这种损伤发生在最小抑制浓度（MIC）下，但在高于MIC的浓度下，其裂解细胞。
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.