Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactions

Enzymatic proteolysis is the key process to produce bioavailable nitrogen in natural terrestrial and aquatic ecosystems for microorganisms and plants. However, little is known on how protein degradation is influenced by organic contaminants. As we known, the overuse of organophosphate esters (OPEs)...

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Main Authors: Zeming Wang, Wei Zhang, Xiaojie Hu, Yanzheng Gao
Format: Article
Language:English
Published: Elsevier 2025-01-01
Series:Environment International
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Online Access:http://www.sciencedirect.com/science/article/pii/S0160412025000078
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author Zeming Wang
Wei Zhang
Xiaojie Hu
Yanzheng Gao
author_facet Zeming Wang
Wei Zhang
Xiaojie Hu
Yanzheng Gao
author_sort Zeming Wang
collection DOAJ
description Enzymatic proteolysis is the key process to produce bioavailable nitrogen in natural terrestrial and aquatic ecosystems for microorganisms and plants. However, little is known on how protein degradation is influenced by organic contaminants. As we known, the overuse of organophosphate esters (OPEs) has caused serious pollution in soil, water, and sediment. Thereby we studied the effect of OPEs on the proteolysis of protein GB1 in aqueous system at neutral pH, and explored the underlying molecular mechanism. Colorimetric ninhydrin methods and SDS-PAGE results revealed that OPEs inhibited the enzymatic hydrolysis of protein GB1. Based on fluorescence quenching experiments, the binding constant (LogKA) were found in order: 6.16 (dibutyl phosphate) > 5.11 (diethyl phosphate) > 1.78 (tributyl phosphate) > 0.876 (triethyl phosphate), proving the interactions between OPEs and protein GB1. Further spectroscopic experiments and molecular docking simulations showed that OPEs could entered the pocket structure of GB1 and induced secondary structural changes and protein folding through non-covalent interactions dominated by hydrogen bonding and van der Waals forces. In addition, organophosphate diesters (di-OPEs) and long-chain OPEs had stronger affinity to GB1, due to the more negative and denser electrostatic surface potential distributions. The deformation of proteins hindered the contact between their active sites and enzymes, leading to the inhibition of GB1 hydrolysis. This study deepened our understanding of the effect of OPEs on protein transformation and degradation, which could further influence the ecological functions and nutrient cycling.
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spelling doaj-art-9de97028a5a94d9ab4268ed1e23587b22025-01-24T04:44:15ZengElsevierEnvironment International0160-41202025-01-01195109256Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactionsZeming Wang0Wei Zhang1Xiaojie Hu2Yanzheng Gao3Institute of Organic Contaminant Control and Soil Remediation, College of Resources and Environmental Sciences, Nanjing Agricultural University, Nanjing, Jiangsu 210095, ChinaDepartment of Plant, Soil and Microbial Sciences, Michigan State University, East Lansing, MI 48824, United StatesInstitute of Organic Contaminant Control and Soil Remediation, College of Resources and Environmental Sciences, Nanjing Agricultural University, Nanjing, Jiangsu 210095, ChinaInstitute of Organic Contaminant Control and Soil Remediation, College of Resources and Environmental Sciences, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China; Corresponding author at: Weigang Road 1, Nanjing 210095, China.Enzymatic proteolysis is the key process to produce bioavailable nitrogen in natural terrestrial and aquatic ecosystems for microorganisms and plants. However, little is known on how protein degradation is influenced by organic contaminants. As we known, the overuse of organophosphate esters (OPEs) has caused serious pollution in soil, water, and sediment. Thereby we studied the effect of OPEs on the proteolysis of protein GB1 in aqueous system at neutral pH, and explored the underlying molecular mechanism. Colorimetric ninhydrin methods and SDS-PAGE results revealed that OPEs inhibited the enzymatic hydrolysis of protein GB1. Based on fluorescence quenching experiments, the binding constant (LogKA) were found in order: 6.16 (dibutyl phosphate) > 5.11 (diethyl phosphate) > 1.78 (tributyl phosphate) > 0.876 (triethyl phosphate), proving the interactions between OPEs and protein GB1. Further spectroscopic experiments and molecular docking simulations showed that OPEs could entered the pocket structure of GB1 and induced secondary structural changes and protein folding through non-covalent interactions dominated by hydrogen bonding and van der Waals forces. In addition, organophosphate diesters (di-OPEs) and long-chain OPEs had stronger affinity to GB1, due to the more negative and denser electrostatic surface potential distributions. The deformation of proteins hindered the contact between their active sites and enzymes, leading to the inhibition of GB1 hydrolysis. This study deepened our understanding of the effect of OPEs on protein transformation and degradation, which could further influence the ecological functions and nutrient cycling.http://www.sciencedirect.com/science/article/pii/S0160412025000078Organophosphate estersProtein GB1ProteolysisNon-covalent interactionMolecular simulation
spellingShingle Zeming Wang
Wei Zhang
Xiaojie Hu
Yanzheng Gao
Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactions
Environment International
Organophosphate esters
Protein GB1
Proteolysis
Non-covalent interaction
Molecular simulation
title Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactions
title_full Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactions
title_fullStr Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactions
title_full_unstemmed Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactions
title_short Organophosphate esters inhibit enzymatic proteolysis through non-covalent interactions
title_sort organophosphate esters inhibit enzymatic proteolysis through non covalent interactions
topic Organophosphate esters
Protein GB1
Proteolysis
Non-covalent interaction
Molecular simulation
url http://www.sciencedirect.com/science/article/pii/S0160412025000078
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AT weizhang organophosphateestersinhibitenzymaticproteolysisthroughnoncovalentinteractions
AT xiaojiehu organophosphateestersinhibitenzymaticproteolysisthroughnoncovalentinteractions
AT yanzhenggao organophosphateestersinhibitenzymaticproteolysisthroughnoncovalentinteractions