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Langmuir. 2014 Apr 15;30(14):4078-83. doi: 10.1021/la500027f. Epub 2014 Mar 31.

Effect of charge regulation and ion-dipole interactions on the selectivity of protein-nanoparticle binding.

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Department of Physics and Chemistry, Faculty of Pharmaceutical Sciences at Ribeirão Preto, University of São Paulo , Ribeirão Preto, SP 14040-903, Brazil.


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 β-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.

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