abstract

• The understanding of the adsorption and interfacial behavior of proteins is crucial to the development of novel biosensors and biomaterials. By using bottom-up atomistic multiscale simulations, we study here the adsorption of lysozyme on Au(111) surfaces in an aqueous environment. Atomistic simulations are used to calculate the inhomogeneous polarization of the gold surface, which is induced by the protein adsorption, and by the presence of an interfacial layer of water molecules and monovalent salts. The corresponding potential of mean force between the protein and the gold surface including polarization effects is used in Langevin Dynamics simulations to study the time dependent behavior of proteins at finite concentration. These simulations display a rapid adsorption and formation of a first-layer of proteins at the interface. Proteins are initially adsorbed directly on the gold surface due to the strong protein-surface attractive interaction. A subsequent interfacial weak aggregation of proteins leading to multilayer build-up is also observed at long times. © 2017 Author(s).

authors

• Guerrero García Guillermo Iván
• Jahan Sajib Md.S.
• Ma H.
• Samieegohar M.
• Sha F.
• Wei T.

publication date

• 2017-01-01

published in

• Applied Physics Letters  Journal

keywords

• Adsorption; Enzymes; Gold; Gold metallurgy; Molecular dynamics; Molecules; Polarization; Aqueous environment; Atomistic simulations; Attractive interactions; Interfacial behaviors; Multi-scale simulation; Polarization effect; Potential of mean force; Time dependent behavior; Proteins

Digital Object Identifier (DOI)

• 10.1063/1.4976516

start page

end page

volume

• 110

issue

• 7