The role of surface energy of technical polymers in serum protein adsorption and MG-63 cells adhesion

Proteins, platelets, and blood coagulation at biomaterial interfaces

“…Calculation of the interfacial energy of protein interaction with surface from the surface free energy of a biomaterial is helpful to quantitatively understand the mechanisms of protein adsorption on varied surfaces 51–53 . It has been reported that there is a correlation between the amount of protein adsorbed on the polymeric materials such as poly(methylmethacrylate) (PMMA), polystyrene (PS), and poly(dimethylsiloxane) (PDMS) and the total surface energy of the substrate, i.e., adsorption is higher on low energy substrates 54 .…”

Influence of Saliva and Mucin on the Adhesion of <i>Candida</i> Oral Clinical Isolates

“…The changes observed in the presence of mucin (in PBS) may be explained by the conformational adaptation and exposure of its hydrophilic terminals [14] [22] when bound to the surface. It is known that, although most proteins adsorb preferentially onto lowenergy surfaces, some proteins, such as albumin, preferentially adsorb on substrates with surface energies that have a high polar (electron donor parameter (γ -)) components [23]. This is a very important result, as it demonstrates the impact on the surface free energy parameters and on the hydrophobicity of the surface (Figure 1(c)) materials in the presence of different substances.…”

Functionalization of Silicone Rubber Surfaces towards Biomedical Applications

“…Recent studies reported poor cell adhesion to PDMS coated with fi bronectin mainly due to the low adsorption effi ciency of fi bronectin to bare PDMS surfaces [117]. Indeed, although some authors found that fi bronectin adsorption is higher for hydrophobic surfaces, this does not necessarily mean a "good" cell interaction [118]; as previously mentioned protein adsorption to hydrophobic surfaces is thermodynamically favorable, but this adsorption can be strong and irreversible, thus denaturing the protein and interfering with its activity. Th is is because the protein's active sites (the epitopes containing GRD sequences) may not be available for proper cell recognition and attachment [115].…”