Interaction study on bovine serum albumin physically binding to silver nanoparticles: Evolution from discrete conjugates to protein coronas

被引:32
作者
Guo, Jun [1 ]
Zhong, Ruibo [1 ]
Li, Wanrong [1 ]
Liu, Yushuang [1 ]
Bai, Zhijun [1 ]
Yin, Jun [1 ]
Liu, Jingran [1 ]
Gong, Pei [1 ]
Zhao, Xinmin [2 ]
Zhang, Feng [1 ]
机构
[1] Inner Mongolia Agr Univ, Sch Life Sci, Agr Nanoctr, Hohhot 010018, Peoples R China
[2] Inner Mongolia Agr Univ, Sch Foreign Language, Hohhot 010018, Peoples R China
基金
中国国家自然科学基金;
关键词
Silver nanoparticle; Bovine serum albumin; Discrete conjugate; Fluorescence quenching; Conformational change; SURFACE-PLASMON RESONANCE; QUANTUM DOTS; IMMUNOMAGNETIC SEPARATION; MAGNETIC SEPARATION; GOLD NANOPARTICLES; FLUORESCENCE; PROBES; SIZE; AU;
D O I
10.1016/j.apsusc.2015.09.247
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The nanostructures formed by inorganic nanoparticles together with organic molecules especially biomolecules have attracted increasing attention from both industries and researching fields due to their unique hybrid properties. In this paper, we systemically studied the interactions between amphiphilic polymer coated silver nanoparticles and bovine serum albumins by employing the fluorescence quenching approach in combination with the Stern-Volmer and Hill equations. The binding affinity was determined to 1.30 x 10(7) M-1 and the interaction was spontaneously driven by mainly the van der Waals force and hydrogen-bond mediated interactions, and negatively cooperative from the point of view of thermodynamics. With the non-uniform coating of amphiphilic polymer, the silver nanoparticles can form protein coronas which can become discrete protein-nanoparticle conjugates when controlling their molar ratios of mixing. The protein's conformational changes upon binding nanoparticles was also studied by using the three-dimensional fluorescence spectroscopy. (C) 2015 Elsevier B.V. All rights reserved.
引用
收藏
页码:82 / 88
页数:7
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