Abstract
Adsorption of human serum albumin on three different soft contact lens surfaces (lathe cut and spin cast crosslinked PHEMA and spin cast PHEMA/MAA) was studied. Using ATR-FTIR spectroscopy the spectra of the adsorbed protein were obtained at different times of adsorption. Structural changes were detected, initially characterized by an increase in hydrogen bonding and after that by involvement of the protein hydrophobic side chain residues. At long adsorption times, the protein becomes denatured, its α-helix content is drastically reduced and the amounts of random coil and β-sheet conformations are increased. ATR-FTI R and circular dichroism studies of albumin solutions reveal similar conformational changes to those experienced by the adsorbed protein. Differences in the adsorption behaviour for the hydrogel surface, indicate the importance of the hydrophilicity, surface regularity and the chemical composition of the contact lens surfaces as the controlling parameters in the protein adsorption phenomena.
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