Protein adsorption on hydrogels. II. Reversible and irreversible interactions between lysozyme and soft contact lens surfaces.
Lysozyme was adsorbed on spin cast and lathe cut soft contact lenses of poly-2-hydroxyethylmethacrylate (PHEMA) and on poly-HEMA-methacrylic acid (PHEMA/MAA). The in vitro adsorption process was followed by ATR-FTIR. Lysozyme adsorbs both, reversibly and irreversibly, on the surfaces. While the reversible bound lysozyme experiences only minor changes in its secondary structure, conformational changes occur for the irreversibly adsorbed protein. The type and extent of structural changes depend on the degree of protein coverage on the lens surface, as well as the chemical structure and surface morphology of the lenses. PHEMA/MAA lenses adsorbed thirty times more lysozyme than either of the PHEMA lenses. Fabrication processes appear to induce different adsorption behaviour, PHEMA lathe cut lenses adsorb twice the amount of protein compared with PHEMA spin cast lenses.
D000327:Adsorption; D002021:Buffers; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003263:Contact Lenses, Hydrophilic; D007700:Kinetics; D009113:Muramidase / Q000032:analysis*; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000032:analysis*
D002021:Buffers; D011506:Proteins; D009113:Muramidase