The sequence-dependent morphology of self-assembly peptides after binding with organophosphorus nerve agent VX  

作　　者：Xiangmin Lei Dingwei Gan Jianan Chen Haochi Liu Jianfeng Wu Jifeng Liu 

机构地区：[1]State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Food Quality and Healthy of Tianjin, College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin, 300457, China [2]School of Electrical Engineering, Xi’an Jiaotong University, Xi’an, 710049, China [3]State Key Laboratory of Toxicology and Medical Countermeasures and Laboratory of Toxicant Analysis, Institute of Pharmacology and Toxicology, Academy of Military Medical Sciences, Beijing, 100850, China

出　　处：《Nano Research》2024年第11期9834-9844,共11页纳米研究（英文版）

基　　金：supported by the National Key R&D Program of China(No.2020YFF0305002);the Project program of Tianjin Key Laboratory of Food Quality and Health,Tianjin University of Science and Technology(No.TJS202102).

摘　　要：VX is a highly toxic organophosphorus nerve agent that the Chemical Weapons Convention classifies as a Schedule 1. In our previous study, we developed a method for detecting organophosphorus compounds using peptide self-assembly. Nevertheless, the self-assembly mechanisms of peptides that bind organophosphorus and the roles of each peptide residue remain elusive, restricting the design and application of peptide materials. Here, we use a multi-scale computational combined with experimental approach to illustrate the self-assembly mechanism of peptide-bound VX and the roles played by residues in different peptide sequences. We calculated that the self-assembly of peptides was accelerated after adding VX, and the final size of assembled nanofibers was larger than the original one, aligning with experimental findings. The atomic scale details offered by our approach enabled us to clarify the connection between the peptide sequences and nanostructures formation, as well as the contribution of various residues in binding VX and assembly process. Our investigation revealed a tight correlation between the number of Tyrosine residues and morphology of the assembly. These results indicate a self-assembly mechanism of peptide and VX, which can be used to design functional peptides for binding and hydrolyzing other organophosphorus nerve agents for detoxification and biomedical applications.

关 键 词：peptide self-assembly molecular dynamic simulation density functional theory organophosphorus nerve agent wave function analysis 

分 类 号：O62[理学—有机化学]