Bovine lactoferrin and its tryptic peptides: Antibacterial activity against different species
Bovine lactoferrin and its tryptic peptides: Antibacterial activity against different species
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DOI：
10.1134/s0003683816040116
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发表时间：
2016-07-01
影响因子：
0.8
通讯作者：
Amicosante, G.
中科院分区：
文献类型：
--
作者：
Lizzi, A. R.;Carnicelli, V.;Amicosante, G.
新型抗菌化合物的研究对许多国家的公共卫生和经济产生了影响。考虑到细菌耐药性的巨大问题，研究绕过这种机制的新分子非常重要。胰蛋白酶是肠道生理学所必需的酶，它形成的肽可能对制药工业有很大的兴趣。在这项研究中，未消化和胰蛋白酶水解的铁耗尽形式的乳铁蛋白（apo-bLf）和未消化和二铁牛乳铁蛋白（bLf）对不同的细菌物种的抗菌活性进行了评价。Apo-bLf对胰蛋白酶水解不太敏感，与二铁形式相比，其分子量低于5000 Da的胰蛋白酶片段具有比从二铁-bLf获得的那些更大的活性。似乎抗菌活性主要通过蛋白质的N-末端部分与细菌细胞的相互作用来发挥。的结构域间的运动，在硅片分析表明，活性的N-末端部分的apo-bLf的构象是更开放的比二铁形式。N-末端区域的可及性增加似乎是负责apo-bLf及其胰蛋白酶片段的抗微生物活性。
The research of new antimicrobial compounds has an impact on public health and economy of many countries. Given the great problem of bacterial resistance, the study of new molecules that bypass this mechanism is of great importance. Trypsin is an enzyme necessary for gut physiology and the peptides it forms could be of great interest to the pharmaceutical industry. In this study the antibacterial activity of undigested and trypsin-hydrolyzed iron-depleted form of lactoferrin, (apo-bLf) and undigested and diferric bovine lactoferrin (bLf) were evaluated against different bacterial species. Apo-bLf was less susceptible to trypsin hydrolysis compared to the diferric form and its tryptic fragments with molecular weight lower than 5000 Da had greater activity than those obtained from the diferric-bLf. It is plausible that the antimicrobial activity is exerted mainly by the interaction of the N-terminal moiety of the protein with the bacterial cell. The in silico analysis of the interdomain movements, showed that the conformation of the active N-terminal part of apo-bLf is more open than that of the diferric form. The increased accessibility of the N-terminal region seems to be responsible for the antimicrobial activity of the apo-bLf and its tryptic fragments.