一种设计肽的所有 l-和 d-氨基酸对映异构体的自组装动力学和抗菌活性。
Self-assembly dynamics and antimicrobial activity of all l- and d-amino acid enantiomers of a designer peptide.
机构信息
MDRCBB, Minnesota Dental Research Center for Biomaterials and Biomechanics, University of Minnesota, Minneapolis, Minnesota 55455, USA.
出版信息
Nanoscale. 2018 Dec 20;11(1):266-275. doi: 10.1039/c8nr07334a.
Recent studies have shown that antimicrobial peptides (AMPs) can self-assemble into supramolecular structures, but this has been overlooked as causative of their antimicrobial activity. Also, the higher antimicrobial potency of d-enantiomers compared to l-enantiomers of AMPs cannot always be attributed to their different resistance to protease degradation. Here, we tested all l- and d-amino acid versions of GL13K, an AMP derived from a human protein, to study structural links between the AMP secondary structure, supramolecular self-assembly dynamics, and antimicrobial activity. pH dependence and the evolution of secondary structures were related to a self-assembly process with differences among these AMPs. The two GL13K enantiomers formed analogous self-assembled twisted nanoribbon structures, but d-GL13K initiated self-assembly faster and had notably higher antimicrobial potency than l-GL13K. A non-antimicrobial scrambled amino acid version of l-GL13K assembled at a much higher pH to form distinctively different self-assembled structures than l-GL13K. Our results support a functional relationship between the AMP self-assembly and their antimicrobial activity.
最近的研究表明，抗菌肽（AMPs）可以自组装成超分子结构，但这一点被忽视了，因为它是 AMP 抗菌活性的原因。此外，与 AMP 的 l-对映体相比，d-对映体的更高抗菌效力并不总是归因于它们对蛋白酶降解的不同抗性。在这里，我们测试了源自人类蛋白的 AMP GL13K 的所有 l-和 d-氨基酸版本，以研究 AMP 二级结构、超分子自组装动力学和抗菌活性之间的结构联系。pH 依赖性和二级结构的演变与自组装过程有关，这些 AMP 之间存在差异。两种 GL13K 对映体形成类似的自组装扭曲纳米带结构，但 d-GL13K 更快地引发自组装，并且抗菌效力明显高于 l-GL13K。l-GL13K 的非抗菌 scrambled 氨基酸版本在更高的 pH 值下组装，形成与 l-GL13K 明显不同的自组装结构。我们的结果支持 AMP 自组装与其抗菌活性之间的功能关系。
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