title: Molecular dynamics simulation of RGD peptide adsorption on titanium oxide surfaces.
abstract: Peptide Arg-Gly-Asp (RGD) sequence is a ubiquitous adhesive motif found in various bone extracellular matrix proteins and is crucial in the biomaterial surface/interface reaction. This study analyzed the adsorption of RGD on different titanium oxide surfaces with molecular dynamics simulation. The simulation results indicate that the RGD peptide binds strongly with anatase (001) and rutile (010). RGD conformation changes due to the variation of the backbone torsion angle in the middle of the RGD chain. Pair correlation function analysis indicates that the interaction of the RGD peptide and the titanium oxide results from hydrogen bonding and the groups in RGD play different roles during the adsorption process. This study provides useful information on how to design titanium surfaces in order to modulate peptide or protein adsorption.
authors.affiliation: School of Materials Science and Engineering, Southwest Jiaotong University, Chengdu, Sichuan, 610031, China.
authors.forename: Hong-Ping
authors.initials: HP
authors.lastname: Zhang
authors.forename: Xiong
authors.initials: X
authors.lastname: Lu
authors.forename: Li-Ming
authors.initials: LM
authors.lastname: Fang
authors.forename: Jie
authors.initials: J
authors.lastname: Weng
authors.forename: Nan
authors.initials: N
authors.lastname: Huang
authors.forename: Yang
authors.initials: Y
authors.lastname: Leng
mesh_terms: D000327:Adsorption; D000595:Amino Acid Sequence; D003198:Computer Simulation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008968:Molecular Conformation; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D013499:Surface Properties; D014025:Titanium / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D009842:Oligopeptides; C009495:titanium dioxide; C047981:arginyl-glycyl-aspartic acid; D014025:Titanium