Effect of Charge Regulation and Ion-Dipole Interactions on the Selectivity of Protein-Nanoparticle Binding

被引：36
作者：
Barroso da Silva, Fernando Luis [1 ]
Bostrom, Mathias [2 ,3 ]
Persson, Clas [2 ,3 ,4 ]
机构：
[1] Univ Sao Paulo, Fac Pharmaceut Sci Ribeirao Preto, Dept Phys & Chem, BR-14040903 Ribeirao Preto, SP, Brazil
[2] Royal Inst Technol, Dept Mat Sci & Engn, SE-10044 Stockholm, Sweden
[3] Univ Oslo, Ctr Mat Sci & Nanotechnol, NO-0316 Oslo, Norway
[4] Univ Oslo, Dept Phys, NO-0316 Oslo, Norway
来源：
LANGMUIR | 2014年 / 30卷 / 14期
基金：
巴西圣保罗研究基金会;
关键词：
SALT; COMPLEXATION; SCIENCE;
D O I：
10.1021/la500027f
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
We investigate the role of different mesoscopic interactions (Coulomb, charge regulation, and ion-dipole "surface patch" effects) on the binding of bovine serum albumin (BSA) and beta-lactoglobulin (BLG) to a cationic gold nanoparticle (TTMA+). The results demonstrate that the charge-regulation mechanism plays a vital role for selectivity of protein-nanoparticle complexation at low salt concentration. At slightly higher ionic strengths, charge-dipole effects are the dominating driving force. Thus, very small variations in salt concentration strongly influence the origin of complexation.
引用
收藏
页码：4078 / 4083
页数：6
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