Molecular design of αvβ3 integrin links to RGD grafted polyethylene provides the estimation of endothelial cell adhesion

Endothelial cell adhesion to a synthetic surface involves a definite set of molecular interactions. Cell adhesion is managed by fibronectin and vitronectin that bind to trans-membrane protein dimers, the integrins. These proteins contain one of the binding sites (I-like-domain) for the Arg-Gly-Asp (RGD) peptides. A molecular approach can allow adhesion strength quantification by ligand-receptor force computation that is a necessary step for the design of peptidomimetic drugs capable of enhancing cell adhesion. The molecular interaction energy between polyethylene surface covalently grafted with the adhesion sites and trans-membrane integrin receptor (I-domain), are evaluated through a molecular model of a single ligand-receptor complex. The work focuses on: 1) Generation of the receptor molecular model; building a model of the I-like domain, the binding site. 2) Evaluation of the greatest binding affinity between the I-like domain and some RGD-containing peptides. 3) Development of the molecular models of the bio-mimetic polyethylene. 4) Evaluation of the interaction energies and the out coming interaction force between the I-like domain and the bio-mimetic material. These interactions can provide an estimation of the adhesion force of a ligand-receptor complex and finally, of endothelial cell adhesion force.