Protein Corona Formation on Cadmium-Bearing Nanoparticles:Important Role of Facet-Dependent Binding of Cysteine-Rich Proteins  

作　　者：Yu Qi Wenyu Guan Chuanjia Jiang Wei Chen Tong Zhang 

机构地区：[1]State Key Laboratory of Environmental Chemistry and Ecotoxicology,Research Center for Eco-Environmental Sciences,Chinese Academy of Sciences,Beijing 100085,People’s Republic of China [2]University of Chinese Academy of Sciences,Beijing 100049,People’s Republic of China [3]College of Environmental Science and Engineering,Ministry of Education Key Laboratory of Pollution Processes and Environmental Criteria,Tianjin Key Laboratory of Environmental Remediation and Pollution Control,Nankai University,Tianjin 300350,People’s Republic of China

出　　处：《Environment & Health》2024年第9期623-630,共8页环境与健康（英文）

基　　金：supported by the National Natural Science Foundation of China(22125603,22276211,and 22193051);Tianjin Municipal Science and Technology Commission(21JCJQJC00060).

摘　　要：Cadmium-bearing nanoparticles,such as nanoparticulate cadmium selenide(CdSe)and cadmium sulfide(CdS),widely exist in the environment and originate from both natural and anthropogenic sources.Risk assessment of these nanoparticles cannot be accurate without taking into account the properties of the protein corona that is acquired by the nanoparticles upon biouptake.Here,we show that the compositions of the protein corona on CdSe/CdS nanoparticles are regulated collectively by the surface atomic arrangement of the nanoparticles and the abundance and distribution of cysteine moieties of the proteins in contact with the nanoparticles.A proteomic analysis shows that the observed facet-dependent preferential binding of proteins is mostly related to the cysteine contents of the proteins,among commonly recognized protein properties controlling the formation of the protein corona.Theoretical calculations further demonstrate that the atomic arrangement of surface Cd atoms,as dictated by the exposed facets of the nanoparticles,controls the specific binding mode of the S atoms in the disulfide bonds of the proteins.Supplemental protein adsorption experiments confirm that disulfide bonds remain intact during protein adsorption,making the binding of protein molecules sensitive to the abundance and distribution of Cd-binding moieties and possibly molecular rigidity of the proteins.The significant conformational changes of adsorbed proteins evidenced from a circular dichroism spectroscopy analysis suggest that disrupting the structural stability of proteins may be an additional risk factor of Cd-bearing nanoparticles.These findings underline that the unique properties and behaviors of nanoparticles must be fully considered when evaluating the biological effects and health risks of metal pollutants.

关 键 词：Heavy metal Mineral nanoparticles Exposed facet Protein corona Preferential adsorption 

分 类 号：TB383[一般工业技术—材料科学与工程]