Effects of Orientation on the Stability and Affinity of Antibody–GNP Conjugation

Abstract

In medicine, gold nanoparticles are widely used because of its unique properties. They are usually attached to a monoclonal antibody in treatment and diagnosis. Computational and laboratory work has demonstrated that the structure of the protein can change after interaction with gold nanoparticle and the effect of nanoparticle on the protein is dependent on the type of bond between them. Thus, finding out how nanoparticles affect the protein structure can help us to design the optimal complex of gold nanoparticle–antibody. In the present study, docking and molecular dynamic simulation were performed to obtain an insight at the molecular level in the binding of immunoglobulin G to the Gold nanoparticles, the structure change in immunoglobulin G, and binding energies of Fab and Fc domains of Immunoglobulin G to the GNP. We found the Fab region was more stable than the Fc region when bound to the GNP surface and it also had less structural changes. In neutral pH, Van der Waals interactions contribute more to the Fab–GNP interaction compared to electrostatic interactions; However, in Fc–GNP interaction, the main contributor is the electrostatic energy.