title: Molecular docking characterization of a four-domain segment of human fibronectin encompassing the RGD loop with hydroxyapatite.
abstract: Fibronectin adsorption on biomaterial surfaces plays a key role in the biocompatibility of biomedical implants. In the current study, the adsorption behavior of the 7-10th type III modules of fibronectin (FN-III7-10) in the presence of hydroxyapatite (HAP) was systematically investigated by using molecular docking approach. It was revealed that the FN-III10 is the most important module among FN-III7-10 in promoting fibronectin binding to HAP by optimizing the interaction energy; the arginine residues were observed to directly interact with the hydroxyl group of HAP through electrostatic forces and hydrogen bonding. Moreover, it was found that the HAP-binding sites on FN-III10 are mainly located at the RGD loop region, which does not affect the interaction between the fibronectin protein and its cognate receptors on the cell surface.
authors.forename: Tailin
authors.initials: T
authors.lastname: Guo
authors.forename: Wenyuan
authors.initials: W
authors.lastname: Kang
authors.forename: Dongqin
authors.initials: D
authors.lastname: Xiao
authors.forename: Rongquan
authors.initials: R
authors.lastname: Duan
authors.forename: Wei
authors.initials: W
authors.lastname: Zhi
authors.affiliation: School of Life Science and Engineering, Southwest Jiaotong University, Chengdu 610031, China. jweng@swjtu.edu.cn.
authors.forename: Jie
authors.initials: J
authors.lastname: Weng
mesh_terms: D001665:Binding Sites; D017886:Durapatite / Q000737:chemistry* / Q000378:metabolism; D005353:Fibronectins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D009842:Oligopeptides / Q000737:chemistry*; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs
chemical_list: D005353:Fibronectins; D009842:Oligopeptides; C047981:arginyl-glycyl-aspartic acid; D017886:Durapatite