Characterization of protein adsorption on soft contact lenses. IV. Comparison of in vivo spoilage with the in vitro adsorption of tear proteins.
Tear protein and gamma-globulin mixtures were adsorbed on soft contact lenses of different chemical composition, surface quality and water content. The adsorption process was followed by Fourier transform infrared-attenuated total reflectance spectroscopy (ATR-FTIR). It was found that gamma-globulin underwent a conformational and orientational change after its adsorption and the extent of structural change appeared to be proportional to the binding strength of the protein with the hydrogel surface. Electrostatic interactions play a major role in the protein adsorption on lenses containing methacrylic acid. Lysozyme is selectively adsorbed on all of the high water content hydrogels and mucin is the major protein component for the pure PHEMA type of lenses. Studies on in vivo spoiled PHEMA and PVP/MMA lenses indicate that lysozyme is the major adsorbed deposit. Papain cleaning of in vivo spoiled lenses shows that although a portion of the deposits is desorbed, the enzyme itself becomes irreversibly adsorbed to the contact lens which may cause harmful effects to the eye.
Castillo
E J
EJ
Koenig
J L
JL
Anderson
J M
JM
D000327:Adsorption; D003263:Contact Lenses, Hydrophilic / Q000009:adverse effects*; D004563:Electrochemistry; D006801:Humans; D066298:In Vitro Techniques; D009113:Muramidase / Q000378:metabolism; D010206:Papain; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*; D013055:Spectrophotometry, Infrared; D013666:Tears / Q000378:metabolism*; D005719:gamma-Globulins / Q000378:metabolism
D011506:Proteins; D005719:gamma-Globulins; D009113:Muramidase; D010206:Papain