牛乳铁素结构和功能研究进展

Development of sturcture and funtion research of bovine lactoferricin

牛乳铁蛋白是一种多功能蛋白质,具有抗菌,抗真菌,抗病毒,抗癌,抗炎,以及免疫调节作用,而这些性质都与其高度碱性的N端区域有关。这部分蛋白能在胃的酸性pH值条件下释放出来,新生成的含有25个氨基酸残基的抗菌肽被称为乳铁素。在本文中综述了该抗菌肽结构,以及结构和功能相互联系。抗菌肽和细胞膜的相互作用表明,同中性的真核细胞膜相比它更容易与带负电荷的细菌细胞膜和癌细胞膜发生反应,肽的结合破坏了膜的正常结构。对乳铁素活性非常重要的残基是色氨酸和精氨酸,他们是使蛋白质或合成抗菌肽类能自然的穿过细胞膜区域的根本原因。同时乳铁素的抗菌,抗真菌,抗病毒,抗癌性质与富含Trp/Arg的区域有关。

Lactoferrin is a multifunctional protein that has antibacterial, antifungal, antiviral, antitumour, anti- inflammatory, and immunoregu- latory properties. All of these properties appear to be related to its highly basic N- terminal region. This part of the protein can be released in the stomach by pepsin cleavage at acid pH. The 25- residue antimicrobial peptide that is released is called lactoferricin. In this paper, we re- view the structure of the peptide and attempt to relate this to its many functions. The interaction of the peptide with cell membranes show that binding to net negatively charged bacterial and cancer cell membranes is preferred over neutral eukaryotic membranes. Residues that are of particular importance for the activity of lactoferricin are tryptophan and arginine, which are regions of proteins or synthetic peptides that can spontaneously cross membranes. At the same time, the antimicrobial, antifungal, antitumour, and antiviral properties of lactoferricin can be re- lated to the Trp/Arg- rich portion of the peptide.