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Molecules 2014, 19(1), 149-158; doi:10.3390/molecules19010149

Molecular Docking Characterization of a Four-Domain Segment of Human Fibronectin Encompassing the RGD Loop with Hydroxyapatite

1
School of Life Science and Engineering, Southwest Jiaotong University, Chengdu 610031, China
2
Key Laboratory of Advanced Technologies of Material, Minister of Education, School of Materials Science and Engineering, Southwest Jiaotong University, Chengdu 610031, China
*
Author to whom correspondence should be addressed.
Received: 24 October 2013 / Revised: 2 December 2013 / Accepted: 11 December 2013 / Published: 23 December 2013
(This article belongs to the Section Medicinal Chemistry)
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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.
Keywords: fibronectin; hydroxyapatite; molecular docking; RGD loop fibronectin; hydroxyapatite; molecular docking; RGD loop
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

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.

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