Molecular dynamics simulation of RGD peptide adsorption on titanium ozide surfaces
Peptide Arg-Gly-Asp (RGD) sequence is a ubiquitous adhesive motif found in various bone extracel lular 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.
Hong-Ping Zhang Xiong Lu Li-Ming Fang Jie Weng Nan Huang Yang Leng
Key Lab of Advanced Technologies of Materials, Ministry of Education, School of Materials Science an Key Lab of Advanced Technologies of Materials, Ministry of Education, School of Materials Science an Department of Mechanical Engineering, Hong Kong University of Science and Technology, Kowloon, Hong
国际会议
广州
英文
1377-1381
2008-11-01（万方平台首次上网日期，不代表论文的发表时间）