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首页> 外文期刊>ChemPlusChem >Subtle Differences in Initial Membrane Interactions Underpin the Selectivity of Small Antimicrobial Peptides
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Subtle Differences in Initial Membrane Interactions Underpin the Selectivity of Small Antimicrobial Peptides

机译：初始膜相互作用的微妙差异基础小抗菌肽的选择性

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摘要

Host-secreted antimicrobial peptides (AMPs) are found in virtually all organisms, often providing innate immunity as the first line of defence against pathogens. Many AMPs kill pathogens by disrupting their cellular membranes and thus are similar to some antibiotic drugs. Likely drug candidate AMPs are found in non-mammalian hosts but are also haemolytic. Thus, it is crucial to understand the origins of membrane specificity and selectivity of the action of these AMPs. In this study, the membrane specificity of action of citropin 1.1, a 16-residue AMP, was studied by using a quartz crystal microbalance on the basis of mass and viscoelasticity changes in comparison to aurein 1.2 (13 residues) and maculatin 1.1 (21 residues). The membrane selectivity was largely reflected in the nature of the initial interaction of the peptide with the membrane. This initial interaction might determine whether the peptide transforms into a membrane-disrupting alpha-helical conformation and highlights subtle differences in the repositioning of this alpha-helical peptide in the membrane, as reflected by the viscoelasticity data, thus signifying the mechanistic pathway to membrane disruption.
机译：宿主分泌的抗微生物肽（AMPs）几乎可以在几乎所有生物体中发现，通常为对抗病原体的第一道防线提供先天免疫。许多安培通过破坏细胞膜来杀死病原体，因此类似于一些抗生素药物。可能的药物候选AMPS在非哺乳动物宿主中发现，但也是溶血。因此，理解膜特异性的起源和这些安培的作用的选择性至关重要。在该研究中，通过基于质量和粘弹性的基于AUREIN 1.2（13个残基）和MURULATIN 1.1（21个残基），通过使用基于质量和粘弹性的石英晶体微稳定进行柑橘素1.1的膜特异性的植物1.1，16-残基AMP。（21个残基）。膜选择性在很大程度上反映在肽与膜的初始相互作用的性质中。该初始相互作用可以确定肽是否转化为膜中断的α-螺旋构象，并突出膜中该α-螺旋肽的重新定位的微妙差异，如粘弹性数据反射，从而使机械途径引起膜破坏。

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