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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Pore formation and the key factors in antibacterial activity of aurein 1.2 and LLAA inside lipid bilayers, a molecular dynamics study
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Pore formation and the key factors in antibacterial activity of aurein 1.2 and LLAA inside lipid bilayers, a molecular dynamics study

机译：孔隙形成和脂质双层内含素1.2和LLAA抗菌活性的关键因素，分子动力学研究

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摘要

Abstract Aurein 1.2 and LLAA are two antimicrobial peptides with different antibacterial activities (LLAA>Aurein 1.2), though their amino acid sequences are similar. In this manuscript, we study the key features for the different antibacterial activities of these peptides using molecular dynamics simulation. We find that in water, both peptides become disordered and LLAA is observed to have higher water-solubility, a feature which may contribute to enhancing its propensity to disrupt the bilayer and thus higher activity. Both peptides are also investigated while they are initially located inside lipid bilayer as a pre-formed vertical channel composed of five parallel copies of each peptide. LLAA demonstrates larger structural deviation from the initial helical structure and also more structural flexibility which is concluded to be a key feature in its stronger activity. In the presence of LLAA, the bilayer order is perturbed more pronouncedly and the number of water molecules penetrating into bilayer is higher. It is shown that stronger electrostatic interactions, more hydrophobic contacts and more hydrogen bonds between lipid and LLAA also lead to stronger activity of LLAA. The simulation results show instability of the barrel-stave pores for our peptides inside lipid bilayers. Graphical abstract Display Omitted Highlights ? Aurein 1.2 and LLAA are two antibacterial peptides with different activities. ? Interaction of both peptides with DPPC bilayer is studied using MD simulation. ? Structural flexibility of LLAA reveals to be a key factor in its higher activity. ? LLAA perturbs bilayer more pronouncedly and causes more water penetration. ? Final arrangement of lipid head groups shows instability of barrel-stave pore.
机译：摘要Aurein 1.2和LLAA是两种具有不同抗菌活性的抗菌肽（LLAA> Aurein 1.2），但它们的氨基酸序列是相似的。在该稿件中，我们使用分子动力学模拟研究这些肽的不同抗菌活性的关键特征。我们发现在水中，两种肽变得无序，并且观察到LLAA具有更高的水溶性，这是有助于提高其破坏双层的倾向并因此有助于破坏双层的倾向并因此有助于造成更高的倾向。还研究了两种肽，同时它们最初位于脂质双层内部，作为由每种肽的五个平行拷贝组成的预先形成的垂直通道。 LLAA展示了与初始螺旋结构的较大结构偏差，并且还具有更大的结构柔韧性，其结论是在其更强大的活动中成为关键特征。在LLAA存在下，双层顺序扰动更明显，渗透到双层的水分子的数量更高。结果表明，较强的静电相互作用，更疏水的触点和脂质和LLAA之间的更多氢键也导致LLAA的较强活性。仿真结果表明，脂质双层内肽的桶铲孔的不稳定性。图形抽象显示省略了亮点？ AUREIN 1.2和LLAA是两种具有不同活性的抗菌肽。还使用MD仿真研究了肽与DPPC双层的相互作用。还LLAA的结构灵活性显示出在较高活动中的关键因素。还LLAA Perturbs Bilayer更加宣称并导致更多的水渗透。还脂质头部的最终排列显示桶塔孔的不稳定性。

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