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Adhesion of protein residues to substituted (111) diamond surfaces: An insight from density functional theory and classical molecular dynamics simulations
Author(s) -
Borisenko Konstantin B.,
Reavy Helen J.,
Zhao Qi,
Abel Eric W.
Publication year - 2007
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.31700
Subject(s) - adhesion , diamond , density functional theory , materials science , molecular dynamics , adsorption , molecule , surface energy , chemical physics , intermolecular force , conformational isomerism , computational chemistry , crystallography , nanotechnology , chemistry , organic chemistry , composite material
Protein‐repellent diamond coatings have great potential value for surface coatings on implants and surgical instruments. The design of these coatings relies on a fundamental understanding of the intermolecular interactions involved in the adhesion of proteins to surfaces. To get insight into these interactions, adhesion energies of glycine to pure and Si and N‐doped (111) diamond surfaces represented as clusters were calculated in the gas phase, using density functional theory (DFT) at the B3LYP/6‐31G* level. The computed adhesion energies indicated that adhesion of glycine to diamond surface may be modified by introducing additional elements into the surface. The adhesion was also found to induce considerable change in the conformation of glycine when compared with the lowest‐energy conformer of the free molecule. In the Si and N‐substituted diamond clusters, notable changes in the structures involving the substituents atoms when compared with smaller parent molecules, such as 1‐methyl‐1‐silaadamantane and 1‐azaadamantane, were detected. Adhesion free energy differences were estimated for a series of representative peptides (hydrophobic Phe‐Gly‐Phe, amphiphilic Arg‐Gly‐Phe, and hydrophilic Arg‐Gly‐Arg) to a (111) diamond surface substituted with different amounts of N, Si, or F, using molecular dynamics simulations in an explicit water environment employing a Dreiding force field. The calculations were in agreement with the DFT results in that adsorption of the studied peptides to diamond surface is influenced by introducing additional elements to the surface. It has been shown that, in general, substitution will enhance electrostatic interactions between a surface and surrounding water, leading to a weaker adhesion of the studied peptides. © 2007 Wiley Periodicals, Inc. J Biomed Mater Res 86A: 1113–1121, 2008