Quantitative study of protein coronas on gold nanoparticles with different surface modifications
Quantitative study of protein coronas on gold nanoparticles with different surface modifications
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DOI：
10.1007/s12274-013-0400-0
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发表时间：
2014-03-01
期刊：
影响因子：
9.9
通讯作者：
Xie, Liming
中科院分区：
文献类型：
--
作者：
Cui, Menghua;Liu, Renxiao;Xie, Liming
蛋白质冠状结构提供了体内纳米材料的生物学特性。利用动态光散射(DLS)和透射电子显微镜(TEM)研究了不同表面修饰的金纳米粒子(AuNPs)对牛血清白蛋白(BSA)、转铁蛋白(TRF)和纤维蛋白原(FIB)的吸附作用。经聚乙二醇(5k)表面修饰后的AuNPs不吸附蛋白质。经非聚乙二醇改性的AuNPs与FIB呈聚集状态。经柠檬酸和硫代乙醇酸表面修饰的AuNPs显示出6~8 nm厚的BSA和TRF冠层(对应于单层或双层蛋白质)，其中BSA和TRF蛋白冠层的微观解离常数在10(-8)~10(-6)M之间。
Protein coronas provide the biological identity of nanomaterials in vivo. Here we have used dynamic light scattering (DLS) and transmission electron microscopy (TEM) to investigate the adsorption of serum proteins, including bovine serum albumin (BSA), transferrin (TRF) and fibrinogen (FIB), on gold nanoparticles (AuNPs) with different surface modifications (citrate, thioglycolic acid, cysteine, polyethylene glycol (PEG, M (w) = 2 k and 5 k)). AuNPs with PEG(5 k) surface modification showed no protein adsorption. AuNPs with non-PEG surface modifications showed aggregation with FIB. AuNPs with citrate and thioglycolic acid surface modifications showed 6-8 nm thick BSA and TRF coronas (corresponding to monolayer or bilayer proteins), in which the microscopic dissociation constants of BSA and TRF protein coronas are in the range of 10(-8) to 10(-6) M.