Au- and Ag-nanoparticles interaction with fibrin protein molecules

¹ Department of Physics, University of Limpopo, South Africa
² DSI/Mintek Nanotechnology Innovation Centre, Advanced Materials Division, Mintek, South Africa

^* Corresponding author: makgoba.walter@gmail.com

Abstract

The interactions of Au- and Ag-nanospheres with fibrin molecules have been investigated using Monte Carlo, density functional theory and molecular dynamics simulations. The negative adsorption energies were recorded whenever fibrin molecules got adsorbed onto either Au- or Ag-nanospheres. Au(55) and Ag(55) nanospheres recorded the most energetically stable adsorption energies of -3.00 and -3.27 eV respectively. Binding distances between the terminal functional group atoms and either Au- or Ag-nanospheres were estimated using the radial distribution functions. Au-H showed shortest bond lengths of 2.37, 2.47, 2.57, and 2.37 Å respectively for Au(19), Au(38), Au(55), and Au(79) nanospheres. Likewise, Ag-H registered the shortest bond lengths of 2.11, 2.45, 2.57, 2.47 Å respectively for Ag(19), Ag(38), Ag(55), and Ag(79) nanospheres. The mean square displacement and diffusion coefficient constants were also used to probe the possibility of H, C, N, and O atoms diffusion into the Au- and Ag-nanospheres matrices. All H, C, N, and O atoms were found to diffuse readily in Au-nanospheres compared to Ag-nanospheres. Au(55) recorded the highest diffusion coefficient constants for the H, C, and N atoms. Ag(79) registered the highest diffusion coefficient constants for H, C, N, and O atoms.