【摘要】 纳米孔是一种有效的探测蛋白质以及蛋白质复合物的工具.蛋白质与纳米孔的相互作用是生物和生物医学领域普遍存在的基础过程.本文通过分析phi29蛋白穿过氮化硅纳米孔产生的电信号,初步实现了单分子层面对蛋白疏水表面的探测.phi29蛋白穿孔过程中独特的"双层事件"以及双层事件深度的比例表明相互作用发生在phi29蛋白的疏水表面.本文提供了一种在蛋白表面定位疏水区域的潜在方法,揭示了疏水相互作用在蛋白和纳米孔的相互作用中扮演着重要的角色.另外,该研究在固态纳米孔探测蛋白表面化学性质等领域也具有巨大的潜在意义.更多还原

【Abstract】 Solid-state nanopore is found to be a promising tool to detect proteins and their complexes. Nanopore-protein interaction is a fundamental and ubiquitous process in biology and medical biotechnology. By translocating phi29 connector protein through silicon nitride nanopores, we demonstrate preliminarily probing the surface hydrophobicity of individual protein at single-molecule resolution. The unique "double-level event" observed in the translocation and the ratio of two current drop levels suggest that the position where the interaction occurs is the hydrophobic surface of the protein. We provide a potential method to locate the hydrophobic region of a specific protein surface. This study is of fundamental significance in revealing the important role that hydrophobic interaction plays in nanopore-protein interaction and holds great potential for detecting local surface chemical property of individual protein using solid-state nanopores.更多还原