| In recent years,as a large number of environmental pollutants have emerged and their emissions have affected human health problems,research on environmental pollutants has gradually attracted people's attention.Most environmental pollutants are toxic and can enter the body through diet and inhalation of indoor and outdoor air.These contaminants may bind proteins and affect the structure and function of proteins.Protein is the main responsibility of human life activities.Without protein,there is no life.Many structures and functions of organisms are related to proteins.There are many types of proteins,including enzymes,hormones,and antibodies.Pepsin is a type of protein that is responsible for most of the digestive activity of the stomach.It is a digestive enzyme that the exogenous substances first come into contact with when they enter the body.Therefore,environmental pollutants may bind to pepsin after entering the body,leading to changes in the structure of pepsin.The study of the interaction between environmental pollutants and pepsin has important implications for the development of chemistry,pharmacy,and life sciences.This paper adopts the fluorescence spectroscopy,ultraviolet-visible spectroscopy,infrared spectroscopy,circular dichroism and molecular docking has carried out the interaction between environmental pollutants and pepsin research work,and explains the combination between environmental pollutants and pepsin.Through the above analysis,the specific research work of this paper is as follows:1.This paper introduces the harms of some environmental pollutants to organisms and the structure and function of proteins,and discusses the research methods and significance of the interaction between environmental pollutants and pepsin.2.A method for detecting the interaction between dicyandiamide and pepsin was developed using spectroscopic measurements and molecular docking simulations.Through the fluorescence quenching analysis,prove that the interaction of DCD and pepsin is a static quenching mechanism.Extinction mechanism.According to the calculated thermodynamic parameters,the hydrophobic force plays a leading role,which is consistent with the results of molecular docking simulation experiments.In addition,the results of UV-vis spectroscopy,FT-IR spectroscopy,Three-dimensional fluorescence spectroscopy,and CD spectroscopy indicate that the interaction of DCD with pepsin has a certain influence on the secondary structure of pepsin.These studies validate the transport and distribution of DCD at the molecular level andhelp determine its toxicological effects.3.To simulate the physiological conditions of the human body,a method for detecting the interaction between persistent environmental pollutants 3,3',4',4',5-pentachlorobiphenyl(PCB126)and pepsin was proposed.Studies show that the interaction between PCB126 and pepsin is a static quenching mechanism.The results of synchronous fluorescence and three-dimensional fluorescence spectroscopy prove that the addition of PCB126 changes the microenvironment around pepsin and changes the secondary structure of pepsin.Thermodynamic data analysis confirmed that the binding of PCB126 to pepsin was spontaneous.The main role of hydrophobic interactions is consistent with the results of molecular docking studies.4.Based on the interaction mechanism of imidacloprid and pepsin,a method for detecting the effect of neonicotinoid insecticide imidacloprid on pepsin structure was constructed.The use of fluorescence spectroscopy demonstrated that the interaction between imidacloprid and pepsin is a static quenching mechanism,and time-resolved fluorescence further confirms this conclusion.Thermodynamic data analysis confirmed the type of force and was consistent with the results of molecular docking experiments.In addition,the effect of imidacloprid on the secondary structure of pepsin was further confirmed by UV-vis spectroscopy,FT-IR spectroscopy,Three-dimensional fluorescence spectroscopy and CD spectroscopy. |
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