title: Effect of charge regulation and ion-dipole interactions on the selectivity of protein-nanoparticle binding.
abstract: 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.
authors.affiliation: Department of Physics and Chemistry, Faculty of Pharmaceutical Sciences at Ribeirão Preto, University of São Paulo , Ribeirão Preto, SP 14040-903, Brazil.
authors.forename: Fernando Luís
authors.initials: FL
authors.lastname: Barroso da Silva
authors.forename: Mathias
authors.initials: M
authors.lastname: Boström
authors.forename: Clas
authors.initials: C
authors.lastname: Persson
mesh_terms: D001665:Binding Sites; D006046:Gold / Q000737:chemistry*; D007477:Ions / Q000737:chemistry; D007782:Lactoglobulins / Q000737:chemistry*; D053768:Metal Nanoparticles / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D007477:Ions; D007782:Lactoglobulins; D012710:Serum Albumin, Bovine; D006046:Gold