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作 者:Shi-Ya Peng Ya-Di Yang Rong Tian Naihao Lu
出 处:《Journal of Environmental Sciences》2025年第3期88-98,共11页环境科学学报(英文版)
基 金:supported by the National Natural Science Foundation of China(Nos.31960196,31760255,and 82260637);Jiangxi Provincial Natural Science Foundation(No.20212BAB205016).
摘 要:A key characteristic to be elucidated,to address the harmful health risks of environmental perfluorinated alkyl substances(PFAS),is their binding modes to serum albumin,the most abundant protein in blood.Hexafluoropropylene oxide-dimer acid(GenX or HFPO-DA)is a new industrial replacement for the widespread linear long-chain PFAS.However,the detailed interaction of new-generation short-chain PFAS with albumin is still lacking.Herein,the binding characteristics of bovine serum albumin(BSA)to GenX were explored at the molecular and cellular levels.Itwas found that this branched short-chain GenX could bind to BSA with affinity lower than that of legacy linear long-chain perfluorooctanoic acid(PFOA).Site marker competitive study and molecular docking simulation revealed that GenX interacted with subdomain IIIA to form BSA-GenX complex.Consistent with its weaker affinity to albumin protein,the cytotoxicity of branched short-chain GenX was less susceptible to BSA binding compared with that of the linear long-chain PFOA.In contrast to the significant effects of strong BSA-PFOA interaction,the weak affinity of BSA-GenX binding did not influence the structure of protein and the cytotoxicity of GenX.The detailed characterization and direct comparisons of serum albumin interaction with new generation short-chain GenX will provide a better understanding for the toxicological properties of this new alternative.
关 键 词:GenX Protein binding ALBUMIN CYTOTOXICITY Risk assessment
分 类 号:X591[环境科学与工程—环境工程]
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