Bactericidal activity of Lfchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides
Bactericidal activity of Lfchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides
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DOI：
10.1016/j.biochi.2008.05.019
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发表时间：
2009-01-01
期刊：
影响因子：
3.9
通讯作者：
Veerman, Enno C. I.
中科院分区：
文献类型：
--
作者：
Bolscher, Jan G. M.;Adao, Regina;Veerman, Enno C. I.
先天免疫因子乳铁蛋白具有两个抗微生物部分，乳铁蛋白和乳铁蛋白，位于分子的NI结构域中非常接近。最有可能的是，它们在乳铁蛋白的许多有益活动中合作。为了研究两种肽的嵌合是否形成功能单元，我们设计了含有乳铁蛋白氨基酸17-30和乳铁蛋白氨基酸265-284的嵌合结构。发现该LF嵌合体的杀菌活性显著强于组成肽的杀菌活性，如通过需要较低剂量、较短孵育时间和较低离子强度依赖性所证明的。同样，强烈增强与带负电荷的模型膜的相互作用，发现LFchimera相对于组成肽。因此，嵌合的两个抗菌肽类似于其在天然分子中的结构取向显着提高其生物活性。(C)2008年，Elsevier Masson SAS。All rights reserved.
The innate immunity factor lactoferrin harbours two antimicrobial moieties, lactoferricin and lactoferrampin, situated in close proximity in the NI domain of the molecule. Most likely they cooperate in many of the beneficial activities of lactoferrin. To investigate whether chimerization of both peptides forms a functional unit we designed a chimerical structure containing lactoferricin amino acids 17-30 and lactoferrampin amino acids 265-284. The bactericidal activity of this LFchimera was found to be drastically stronger than that of the constituent peptides, as was demonstrated by the need for lower dose, shorter incubation time and less ionic strength dependency. Likewise, strongly enhanced interaction with negatively charged model membranes was found for the LFchimera relative to the constituent peptides. Thus, chimerization of the two antimicrobial peptides resembling their structural orientation in the native molecule strikingly improves their biological activity. (C) 2008 Elsevier Masson SAS. All rights reserved.