Farnaud Sebastien, Evans Robert W
Metalloprotein Research Group, Randall Centre for Molecular Mechanisms of Cell Function, King's College London, 3.6 A New Hunt's House, Guy's Campus, London SE1 1UL, UK.
Mol Immunol. 2003 Nov;40(7):395-405. doi: 10.1016/s0161-5890(03)00152-4.
Lactoferrin is a member of the transferrin family of iron-binding proteins. Numerous functions have been reported and continue to be reported for the protein, some of which are related to its iron-binding properties. Its extensive antimicrobial activities were originally attributed to its ability to sequester essential iron, however, it is now established that it possesses bactericidal activities as a result of a direct interaction between the protein or lactoferrin-derived peptides. This article reviews the antimicrobial activities of lactoferrin and discusses the potential mode of action of lactoferrin-derived cationic peptides against Gram-negative bacteria in the light of recent studies.
乳铁蛋白是铁结合蛋白转铁蛋白家族的成员。该蛋白已被报道具有众多功能,且不断有新的功能被发现,其中一些功能与其铁结合特性相关。其广泛的抗菌活性最初被认为归因于其螯合必需铁的能力,然而,现在已经确定,由于该蛋白或乳铁蛋白衍生肽之间的直接相互作用,它具有杀菌活性。本文综述了乳铁蛋白的抗菌活性,并根据最近的研究讨论了乳铁蛋白衍生的阳离子肽对革兰氏阴性菌的潜在作用模式。