Gold nanoparticle effects on the protein corona by docking and molecular dynamic

Upon entering biological systems such as the bloodstream, nanoparticles form molecular complexeswith encountered proteins termed as the protein corona which shields the surface of the exogenousnanoparticle. Blood more abundant proteins such as albumin initially occupy the nanoparticle surface. Due tothe high application of gold nanoparticle in medicine, in this study the docking of human serum albumin isperformed to the gold nanoparticle and followed by investigating the changes in the structure of the protein bymolecular dynamic simulation and GOLP force field. The results revealed that after the adsorption of albuminon the gold nanoparticle, human serum albumin was denatured and alpha-helix amount decreasedsignificantly. Domain III that has a large cavity of fatty acid binding site, plays an important role in adsorptionon the gold nanopoarticle. Lys464, Thr504, Phe505 and Leu581are crucial amino acids inHSA adsorption onthe GNP. After the adsorption of albumin on the gold nanoparticle surface, fluctuations in some domains ofthe protein increased. Variations in helix properties such as helix length, dipole, radius, average phi and psiangles and the length of hydrogen bonds were calculated in details.

Keywords:

protein , interaction , nanotechnology , GOLP , force field , molecular dynamic , docking