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首页> 外文期刊>Biochemistry >Lipid II Induces a Transmembrane Orientation of the Pore-Forming Peptide Lantibiotic Nisin.
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Lipid II Induces a Transmembrane Orientation of the Pore-Forming Peptide Lantibiotic Nisin.

机译：脂质II诱导毛孔形成肽羊毛硫抗生素乳链菌肽的跨膜方向。

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摘要

Nisin is an antimicrobial peptide produced by Lactococcus lactis and used as a food preservative in dairy products. The peptide kills Gram-positive bacteria via the permeabilization of the membrane, most probably via pore formation using the cell wall precursor Lipid II as its docking molecule. In this study, site-directed tryptophan spectroscopy was used to determine the topology of nisin in the Lipid II containing membrane, as a start to elucidate the mechanism of targeted pore formation. Three single tryptophan mutants were used, which are viable representatives of the wild-type peptide. The emission spectra of tryptophans located at the N-terminus, the center, and the C-terminus as well as quenching by acrylamide and spin-labeled lipids were investigated using model membrane vesicles composed of DOPC containing 1 mol % Lipid II. Nisin was shown to adopt an orientation where the most probable position of the N-terminus was found to be near the Lipid II headgroup at the bilayer surface, the position of the center of nisin was in the middle of the phospholipid bilayer, and the C-terminus was located near the interface between the headgroups and acyl chain region. These results were used to propose a model for the orientation of nisin in Lipid II containing membranes. Our findings demonstrated that Lipid II changes the overall orientation of nisin in membranes from parallel to perpendicular with respect to the membrane surface. The stable transmembrane orientation of nisin in the presence of Lipid II might allow us to determine the structure of the nisin-Lipid II pores in the lipid bilayer.
机译：乳链菌肽是乳酸乳球菌产生的抗菌肽，并用作乳制品中的食品防腐剂。该肽通过膜的通透性杀死革兰氏阳性细菌，最有可能通过使用细胞壁前体脂质II作为其对接分子的孔形成来杀死。在这项研究中，定点色氨酸光谱用于确定包含脂质II的膜中乳链菌肽的拓扑结构，以此作为阐明靶孔形成机理的开端。使用了三个单一的色氨酸突变体，它们是野生型肽的可行代表。使用由含有1 mol％脂质II的DOPC组成的模型膜囊泡研究位于N端，中心和C端的色氨酸的发射光谱以及丙烯酰胺和自旋标记脂质的猝灭作用。乳酸链球菌素显示出一种取向，其中N末端的最可能位置位于双层表面的脂质II头基附近，乳酸链球菌素中心的位置位于磷脂双层的中间，而C -末端位于头基和酰基链区域之间的界面附近。这些结果被用来为乳链菌肽在含脂质II的膜中的取向提出模型。我们的发现表明，脂质II可将乳链菌肽在膜中的整体方向从相对于膜表面的平行更改为垂直。在脂质II存在下乳链菌肽的稳定跨膜取向可能使我们能够确定脂质双层中乳链菌肽-脂质II孔的结构。

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