%0 Journal Article
%T Molecular Docking Characterization of a Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop with Hydroxyapatite
%A Tailin Guo
%A Wenyuan Kang
%A Dongqin Xiao
%A Rongquan Duan
%A Wei Zhi
%A Jie Weng
%J Molecules
%D 2014
%I MDPI AG
%R 10.3390/molecules19010149
%X 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¨C10th type III modules of fibronectin (FN-III 7¨C10) in the presence of hydroxyapatite (HAP) was systematically investigated by using molecular docking approach. It was revealed that the FN-III 10 is the most important module among FN-III 7¨C10 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-III 10 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.
%K fibronectin
%K hydroxyapatite
%K molecular docking
%K RGD loop
%U http://www.mdpi.com/1420-3049/19/1/149