Chen Hsiao-Ling, Yen Chih-Ching, Lu Chien-Yu, Yu Chia-Hen, Chen Chuan-Mu
Department of Molecular Biotechnology, Da-Yeh University, Changhwa, Taiwan.
J Agric Food Chem. 2006 May 3;54(9):3277-82. doi: 10.1021/jf053031s.
Lactoferricins are positively charged, highly basic peptides that are generated upon gastric pepsin cleavage of various lactoferrins. In the past decade, there has been active investigation of the key antimicrobial segments of the various shorter synthetic bovine and human lactoferricins, but not in porcine lactoferricin. These studies have demonstrated the distinct solution structures of lactoferricin in bovine and human and established the multifunctional nature of the antibacterial, antifungal, antiendotoxin, and antiviral activities of lactoferricins. However, the protective effects of porcine lactoferricins have yet to be elucidated. In the present study, a series of synthetic derivatives of porcine, bovine, and human lactoferricins with 20-residue and 9-residue peptides were prepared to investigate their antimicrobial nature. We found that the 20-residue porcine lactoferricin (LFcin P-20) displayed antimicrobial activity against Escherichia coli ATCC25922, Staphylococcus aureus ATCC25923, and Candida albicans ATCC14053. The minimal inhibitory concentrations and minimal bactericidal concentrations of LFcin P-20 ranged from 12 to 25 microM when tested in bacteria and fungi. LFcin P-20 was 4 times more effective than human lactoferricin (LFcin H-20), but slightly less effective than bovine lactoferricin (LFcin B-20).
乳铁传递蛋白肽是带正电荷的、高度碱性的肽,由各种乳铁蛋白经胃蛋白酶切割产生。在过去十年中,人们积极研究了各种较短的合成牛和人乳铁传递蛋白肽的关键抗菌片段,但未对猪乳铁传递蛋白肽进行研究。这些研究揭示了牛和人乳铁传递蛋白肽不同的溶液结构,并证实了乳铁传递蛋白肽具有抗菌、抗真菌、抗内毒素和抗病毒等多种功能。然而,猪乳铁传递蛋白肽的保护作用尚未阐明。在本研究中,制备了一系列含20个残基和9个残基肽的猪、牛和人乳铁传递蛋白肽的合成衍生物,以研究它们的抗菌特性。我们发现,含20个残基的猪乳铁传递蛋白肽(LFcin P - 20)对大肠杆菌ATCC25922、金黄色葡萄球菌ATCC25923和白色念珠菌ATCC14053具有抗菌活性。在细菌和真菌中进行测试时,LFcin P - 20的最小抑菌浓度和最小杀菌浓度范围为12至25微摩尔。LFcin P - 20的效果比人乳铁传递蛋白肽(LFcin H - 20)高4倍,但比牛乳铁传递蛋白肽(LFcin B - 20)略低。