title: Protein selective adsorption properties of a polyethylene terephtalate artificial ligament grafted with poly(sodium styrene sulfonate) (polyNaSS): correlation with physicochemical parameters of proteins.
abstract: Immediately after surgical placement of biomaterials, a first step consists in the adsorption of proteins from the biological environment on the artificial surfaces. Because the composition of the adsorbed protein layer modulates the cell response to the implanted material, researchers in the biomaterials field have focused on coating proteins or peptides onto surfaces to improve cell response and therefore the long-term compatibility of the implant. However, some materials used in tissue engineering, mainly synthetic polymers, are too hydrophobic to allow the optimal adsorption of proteins and have to be first submitted to physical or chemical treatments. In our laboratory, we have demonstrated that grafting of poly(sodium styrene sulfonate) (polyNaSS) onto biomaterials can strongly modulate the protein adsorption and the cellular response compared to unmodified surfaces. In this study, we used a liquid chromatography strategy coupled to proteomics to evaluate the adsorptive properties of a polyethylene terephtalate (PET) artificial ligament grafted with polyNaSS, and to identify and analyse proteins adsorbed on PET fibers. Results obtained with platelet rich plasma (PRP) proteins demonstrated that grafting significantly increases the protein adsorption of the PET and also selectively modulates the adsorption of proteins on PET fibers. Finally, regarding physicochemical parameters calculated from the amino acid sequence of identified proteins, we found that the aliphatic index is highly correlated with the selective adsorption of proteins onto the polyNaSS/PET surface. Therefore, the proteomic approach complemented with physicochemical property evaluation could provide a powerful tool for the elaboration of new biomaterials based on protein layer deposition.
authors.affiliation: Université Paris 13-UMR CNRS 7244-CSPBAT-LBPS-UFR SMBH, Bobigny, France.
authors.forename: S
authors.initials: S
authors.lastname: Lessim
authors.forename: S
authors.initials: S
authors.lastname: Oughlis
authors.forename: J J
authors.initials: JJ
authors.lastname: Lataillade
authors.forename: V
authors.initials: V
authors.lastname: Migonney
authors.forename: S
authors.initials: S
authors.lastname: Changotade
authors.forename: D
authors.initials: D
authors.lastname: Lutomski
authors.forename: F
authors.initials: F
authors.lastname: Poirier
mesh_terms: D000327:Adsorption; D001665:Binding Sites; D001672:Biocompatible Materials / Q000138:chemical synthesis*; D001798:Blood Proteins / Q000737:chemistry*; D008422:Materials Testing; D053657:Platelet-Rich Plasma / Q000737:chemistry*; D011093:Polyethylene Terephthalates / Q000737:chemistry*; D011108:Polymers / Q000138:chemical synthesis*; D011485:Protein Binding; D013451:Sulfonic Acids / Q000138:chemical synthesis*
chemical_list: D001672:Biocompatible Materials; D001798:Blood Proteins; D011093:Polyethylene Terephthalates; D011108:Polymers; D013451:Sulfonic Acids; C077114:styrenesulfonic acid polymer