文献类型：期刊文献

英文题名：Single Molecule Study of Hydrogen Bond Interactions Between Single Oligonucleotide and Aerolysin Sensing Interface

作者：Li, Meng-Yin[1];Wang, Ya-Qian[1];Lu, Yao[1];Ying, Yi-Lun[1,2];Long, Yi-Tao[1,2]

机构：[1]East China Univ Sci & Technol, Sch Chem & Mol Engn, Shanghai, Peoples R China;[2]Nanjing Univ, Sch Chem & Chem Engn, State Key Lab Analyt Chem Life Sci, Nanjing, Jiangsu, Peoples R China

年份：2019

卷号：7

外文期刊名：FRONTIERS IN CHEMISTRY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000478017600002)】；

基金：This research was supported by the National Natural Science Foundation of China (21834001 and 61871183), Y-LY is sponsored by National Ten Thousand Talent Program for young top-notch.

语种：英文

外文关键词：single-molecule interface; oligonucleotide; nanopore; hydrogen bond; nanoconfinement

摘要：The aerolysin nanopore displays a charming sensing capability for single oligonucleotide discrimination. When reading from the electrochemical signal, stronger interaction between the aerolysin nanopore and oligonucleotide represent prolonged duration time, thereby amplifying the hidden but intrinsic signal thus improving the sensitivity. In order to further understand and optimize the performance of the aerolysin nanopore, we focus on the investigation of the hydrogen bond interaction between nanopore, and analytes. Taking advantage of site-direct mutagenesis, single residue is replaced. According to whole protein sequence screening, the region near K238 is one of the key sensing regions. Such a positively charged amino acid is then mutagenized into cysteine and tyrosine denoted as K238C, and K238Y. As (dA)(4) traverses the pores, K238C dramatically produces a six times longer duration time than the WT aerolysin nanopore at the voltage of +120 mV. However, K238Y shortens the dwell time which suggests the acceleration of the translocation causing poor sensitivity. Referring to our previous findings in K238G, and K238F, our results suggest that the hydrogen bond does not dominate the dynamic translocation process, but enhances the interaction between pores and analytes confined in such nanopore space. These insights give detailed information for the rational design of the sensing mechanism of the aerolysin nanopore, thereby providing further understanding for the weak interactions between biomolecules and the confined space for nanopore sensing.