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.
Highlights
Fibronectin (FN) is a prominent component of extracellular matrices (ECM) and is present at high concentrations (~300 mg/mL) in plasma
A majority of integrin-mediated interactions of FN with cells occur through the cell binding triplet Arg-Gly-Asp (RGD loop)
The biocompatibility of an implant is related to how the adhering cells interact with the implant surface when the implant is inserted into the body [9]
Summary
Fibronectin (FN) is a prominent component of extracellular matrices (ECM) and is present at high concentrations (~300 mg/mL) in plasma. The biocompatibility of an implant is related to how the adhering cells interact with the implant surface when the implant is inserted into the body [9] These cellular responses are in turn influenced by proteins adsorbing on the implant from the body fluids. The interaction mechanism of FN-III7–10, which contains the RGD loop, with HAP molecules was investigated systematically by using a molecular docking strategy. The binding sites in the RGD loop region of FNIII10 and the influence of FNIII10 on the binding of other modules to HAP were characterized in detail for its great importance in promoting cell adsorption
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