纳米狭缝中Aβ蛋白构象变化的间距作用  

Conformational Changes of AβProtein in Nano-slits

作　　者：王磊[2] 王艳红[1,3] 武京治[1,3] 李孟委[3] WANG Lei;WANG Yan-Hong;WU Jing-Zhi;LI Meng-Wei(School of Information and Communication Engineering,North University of China,Taiyuan 030051,China;School of Chemistry and Chemical Engineering,North University of China,Taiyuan 030051,China;Academy for Advanced Interdisciplinary Research,North University of China,Taiyuan 030051,China)

机构地区：[1]中北大学信息与通信工程学院,太原030051 [2]中北大学化学与化工学院,太原030051 [3]中北大学前沿交叉科学技术研究院,太原030051

出　　处：《生物化学与生物物理进展》2023年第6期1466-1472,共7页Progress In Biochemistry and Biophysics

基　　金：国防科技创新特区(02-ZT-008)资助项目。

摘　　要：目的 金属表面对蛋白质分子具有吸附作用,然而在纳米尺度内,蛋白质分子构象受到狭缝的间距作用尚未明确。本文通过在分子动力学模拟中建立不同间距的金原子层,研究纳米级金属狭缝中蛋白质分子构象变化。方法 使用GOIPCHARMM力场在Au (111)金原子界面间对Aβ1-42蛋白单体进行分子动力学仿真,研究无狭缝的水溶液环境下和由5.0、5.5以及8.5 nm狭缝结构与Aβ蛋白相互作用及蛋白质构象变化。结果 当金狭缝结构间距从5.0 nm增加到8.5 nm,Aβ蛋白分子与两侧金层相互作用可由单表面吸附、双表面吸附过渡到无吸附。结论 Aβ蛋白分子在金狭缝结构中与表面发生相互作用,随狭缝间距和蛋白质分子距界面距离的变化,蛋白质分子的状态可能表现为单表面吸附、双表面吸附和无吸附3种状态。Objective Understanding the dynamics of protein adsorption at the aqueous gold interface is key to advancing the development of many applications based on gold nanostructures such as plasmonic sensors and biomedical materials.However,the protein conformation in metallic nano-slits has not been fully studied.In this paper,the spacing effect of protein conformation changes in gold nano-slits is studied by building gold atomic layers with different nano-slits using molecular dynamics simulations.Methods We used GOIP-CHARMM force fields with GROMACS to simulate the dynamics of Aβ1-42 protein monomers between Au(111)gold atomic interfaces to study the dynamics of Aβprotein and conformational changes in aqueous environments,5.0 nm nano-slit,5.5 nm nano-slit and 8.5 nm nano-slit.Results When the nano-slit spacing is increased from 5.0 nm to 8.5 nm,the interaction of Aβprotein with the gold interface is varied from double-interface adsorption,single-side interface adsorption to no adsorption.Conclusion The interaction of Aβprotein with the metallic interface is greatly affected by the spacing of gold nano-slits.As the slit spacing and the distance of the protein from the interface changes,the protein could exhibit 3 distinct states:single-side surface adsorption,two interface adsorption and no adsorption.We anticipate that the dynamic features of protein adsorption to Au(111)interfaces of nano-slits showed in this work can be extended to other nanostructures and proteins.The results could find applications in design of biosensors for diagnosis of Alzheimer’s disease.

关 键 词：淀粉样蛋白 分子动力学 分子构象 

分 类 号：Q518.4[生物学—生物化学] Q615