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.
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Guo, T.; Kang, W.; Xiao, D.; Duan, R.; Zhi, W.; Weng, J. Molecular Docking Characterization of a Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop with Hydroxyapatite. Molecules 2014, 19, 149-158.
Guo T, Kang W, Xiao D, Duan R, Zhi W, Weng J. Molecular Docking Characterization of a Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop with Hydroxyapatite. Molecules. 2014; 19(1):149-158.
Guo, Tailin; Kang, Wenyuan; Xiao, Dongqin; Duan, Rongquan; Zhi, Wei; Weng, Jie. 2014. "Molecular Docking Characterization of a Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop with Hydroxyapatite." Molecules 19, no. 1: 149-158.