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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Effect of phosphatidylcholine bilayer thickness and molecular order on the binding of the antimicrobial peptide maculatin 1.1
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Effect of phosphatidylcholine bilayer thickness and molecular order on the binding of the antimicrobial peptide maculatin 1.1

机译：磷脂基双层厚度和分子序对抗微生物肽多蛋白的结合的影响1.1

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Abstract Antimicrobial peptides (AMPs) interact directly with bacterial membrane lipids. Thus, changes in the lipid composition of bacterial membranes can have profound effects on the activity of AMPs. In order to understand the effect of bilayer thickness and molecular order on the activity of AMPs, the interaction of maculatin 1.1 (Mac1.1) with phosphatidylcholine (PC) model membranes composed of different monounsaturated acyl chain lengths between 14 and 22 carbons was characterised by dual polarisation interferometry (DPI) and 31P and 1H solid-state NMR techniques. The thickness and bilayer order of each PC bilayer showed a linear dependence on the acyl chain length. The binding of Mac1.1 exhibited a biphasic dependency between the amount of bound Mac1.1 and bilayer thickness, whereby the mass of bound peptide increased from C14 to C16 and then decreased from C16 to C22. Significant perturbation of 31P chemical shift anisotropy (CSA) values was only observed for DOPC (C18) and DEPC (C22), respectively. In the case of DEPC, the greater range in CSA indicated different headgroup conformations or environments in the presence of Mac1.1. Overall, the results indicated that there is a significant change in the bilayer order upon binding of Mac1.1 and this change occurred in a co-operative manner at higher concentrations of Mac1.1 with increasing bilayer thickness and order. Overall, an optimum bilayer thickness and lipid order may be required for effective membrane perturbation by Mac1.1 and increasing the bilayer thickness and order may counteract the activity of Mac1.1 and play a role in antimicrobial resistance to AMPs. Graphical abstract Display Omitted Highlights ? The effect of bilayer thickness and order on the activity of maculatin 1.1 was studied by DPI and NMR. ? The mass of bound peptide was higher for thinner bilayers. ? Binding of maculatin 1.1 causes a significant change in the bilayer order. ? Increases in acyl chain length, bilayer thickness and lipid order impede insertion of Mac1.1 into the membrane.
机译：摘要抗菌肽肽（AMPS）直接与细菌膜脂质相互作用。因此，细菌膜的脂质组合物的变化可以对安培的活性产生深远的影响。为了了解双层厚度和分子序对AMPS活性的影响，通过14至22个碳之间的不同单不饱和酰基链长度组成的磷脂素1.1（MAC1.1）与磷脂酰胆碱（PC）模型膜的相互作用的特征双偏振干涉法（DPI）和31P和1H固态NMR技术。每个PC双层的厚度和双层顺序显示对酰基链长度的线性依赖性。 MAC1.1的结合在结合的MAC1.1和双层厚度之间表现出双相依赖性，由此从C14至C16增加的结合肽的质量从C16降低至C22。仅针对DOPC（C18）和DEPC（C22）观察到31P化学移位各向异性（CSA）值的显着扰动。在DEPC的情况下，CSA中的越大范围在MAC1.1存在下指示不同的头组符合构象或环境。总的来说，结果表明，在MAC1.1的结合时，双层顺序存在显着变化，并且这种变化以较高浓度的MAC1.1以较高的双层厚度和顺序发生这种变化。总的来说，可能需要最佳双层厚度和脂质顺序通过MAC1.1进行有效膜扰动，并增加双层厚度和顺序可以抵消MAC1.1的活性，并在抗微生物抗性对AMPS中发挥作用。图形抽象显示省略了亮点？通过DPI和NMR研究了双层厚度和对微蛋白1.1活性的顺序的影响。还对于较薄的双层的结合肽质量较高。还Mululatin 1.1的结合导致双层顺序发生重大变化。还酰基链长度增加，双层厚度和脂质顺序妨碍将MAC1.1插入膜中。

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