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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Gold / chemistry*
  • Ions / chemistry
  • Lactoglobulins / chemistry*
  • Metal Nanoparticles / chemistry*
  • Serum Albumin, Bovine / chemistry*
  • Surface Properties


  • Ions
  • Lactoglobulins
  • Serum Albumin, Bovine
  • Gold