Monolayer protein adsorption on cationic gold nanoparticles: A thermodynamic study

被引：1
|
作者：
Saikia, Sourav [1 ]
Das, Puspendu K. [1 ]
机构：
[1] Indian Inst Sci, Dept Inorgan & Phys Chem, Bangalore 560012, India
来源：
CHEMICAL PHYSICS LETTERS | 2023年 / 825卷
关键词：
Protein; Adsorption; Gold nanoparticles; Free energy change; Entropy change; EGG-WHITE LYSOZYME; SIZE;
D O I：
10.1016/j.cplett.2023.140595
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 mechanism for adsorption of Lysozyme (Lyz) and cytochrome c (Cyt. c) proteins on cetyltrimethylammonium bromide (CTAB) capped cationic gold nanoparticles (GNPs) of 26, 46, and 68 nm at pH 6.8 were probed by second harmonic light scattering technique (SHLS). We found that both the proteins binds with cationic GNPs with surprisingly high binding constant of 109-1010 M-1. The nsat values clearly indicates that both the proteins form only monolayer on the GNP surface. Dynamic light scattering measurements validate the adsorption parameters obtained from SHLS. The temperature-dependent SHLS measurements revealed that the adsorption processes were favoured by huge entropic gain.
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页数：8
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