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

Molecules

Tailin Guo²  Wenyuan Kang²  Dongqin Xiao¹  Rongquan Duan¹  Wei Zhi¹ 

[1] Key Laboratory of Advanced Technologies of Material, Minister of Education, School of Materials Science and Engineering, Southwest Jiaotong University, Chengdu 610031, China;School of Life Science and Engineering, Southwest Jiaotong University, Chengdu 610031, China

关键词: fibronectin;    hydroxyapatite;    molecular docking;    RGD loop;   

DOI  :  10.3390/molecules19010149

来源: mdpi

【 摘 要 】

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-III_7–10) 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-III_7–10 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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.