Measuring Binding Kinetics of Antibody-Conjugated Gold Nanoparticles with Intact Cells

Small. 2015 Aug;11(31):3782-8. doi: 10.1002/smll.201500112. Epub 2015 Apr 11.


Antibody-conjugated nanomaterials have attracted much attention because of their applications in nanomedicine and nanotheranostics, and amplification of detection signals. For many of these applications, the nanoconjugates must bind with a cell membrane receptor (antigen) specifically before entering the cells and reaching the final target, which is thus important but not well understood. Here, a plasmonic imaging study of the binding kinetics of antibody-conjugated gold nanoparticles with antigen-expressing cells is presented, and the results are compared with that of the nanoparticle-free antibody. It is found that the nanoconjugates can significantly affect the binding kinetics compared with free antibody molecules, depending on the density of the antibody conjugated on the nanoparticles, and expressing level of the antigen on the cell membrane. The results are analyzed in terms of a transition from monovalent binding model to a bivalent binding model when the conjugation density and expressing level increase. These findings help optimize the design of functional nanomaterials for drug delivery and correct interpretation of data obtained with nanoparticle signal amplification.

Keywords: binding kinetics; membrane proteins; nanomedicine; plasmonics.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal / chemistry*
  • Cell Line
  • Cell Line, Tumor
  • Cell Membrane / metabolism
  • Drug Delivery Systems
  • Gold / chemistry*
  • Humans
  • Kinetics
  • Metal Nanoparticles / chemistry*
  • Nanoconjugates / chemistry
  • Nanomedicine
  • Nanostructures / chemistry
  • Perfusion
  • Protein Binding
  • Receptor, ErbB-2 / chemistry
  • Surface Properties
  • Trastuzumab / chemistry


  • Antibodies, Monoclonal
  • Nanoconjugates
  • Gold
  • ERBB2 protein, human
  • Receptor, ErbB-2
  • Trastuzumab