乳铁蛋白
埃德曼退化
肽
防御素
半胱氨酸
肽序列
生物化学
抗菌剂
胃蛋白酶
化学
微生物学
生物
酶
基因
作者
Wayne Bellamy,Mitsunori Takase,Koji Yamauchi,Hiroyuki Wakabayashi,Kouzou Kawase,Mamoru Tomita
标识
DOI:10.1016/0167-4838(92)90346-f
摘要
We report the existence of a previously unknown antimicrobial domain near the N-terminus of lactoferrin in a region distinct from its iron-binding sites. A single active peptide representing this domain was isolated following gastric pepsin cleavage of human lactoferrin, and bovine lactoferrin, and sequenced by automated Edman degradation. The antimicrobial sequence was found to consist mainly of a loop of 18 amino acid residues formed by a disulfide bond between cysteine residues 20 and 37 of human lactoferrin, or 19 and 36 of bovine lactoferrin. Synthetic analogs of this region similarly exhibited potent antibacterial properties. The active peptide of bovine lactoferrin was more potent than that of human lactoferrin having effectiveness against various Gram-negative and Gram-positive bacteria at concentrations between 0.3 μM and 3.0 μM, depending on the target strain. The effect of the isolated domain was lethal causing a rapid loss of colony-forming capability. Our studies suggest this domain is the structural region responsible for the bactericidal properties of lactoferrin.
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