【作者】 李明娟； 赵莹莹； 郭艳丽； 亢晓峰；

【Author】 Mingjuan Li;Yingying Zhao;Yanli Guo;Xiaofeng Kang;Key Laboratory of Synthetic and Natural Functional Molecular Chemistry, College of Chemistry and Materials Science, Northwest University;

【机构】 合成与天然功能分子化学教育部重点实验室西北大学化学与材料科学学院；

【摘要】 蛋白质穿过生物膜过程涉及蛋白-蛋白和蛋白-孔的相互作用[1]。由于穿孔机制比较复杂,在单分子水平上蛋白质-孔相互作用的全面理解仍然缺失[2]。本文基于纳米孔单分子技术,对蛋白质和α-溶血素纳米孔的相互作用进行了深入研究,通过改变α-溶血素的突变位点、装配环糊精适配体以及改变检测电压和pH等条件探索了蛋白-孔之间的相互作用机制,并对这一过程中的熵变化和静电相互作用进行了探讨。这种单分子方法为快速、简便的研究蛋白质-孔之间的相互作用提供了新的途径。更多还原

【Abstract】 Protein translocation across biological membranes process involves protein-protein and protein-pore interactions. A comprehensive understanding of the protein-pore interaction at single-molecule resolution is still missing due to the considerable complexity in the translocation machineries. Here, we show that the interactions between protein and α-hemolysin nanopores were studied in detail based on nanopore technology. The interactions were explored by changing the mutation site of α-hemolysin, assembling adapters, altering voltage and pH experimental conditions. The entropy change and electrostatic interaction in this process are discussed. This single-molecule recording represents a powerful approach to analyze protein-pore interactions.更多还原