Human serum albumin adsorption on hydrogel contact lenses in vitro.

PURPOSE

To improve the understanding of the formation of protein deposits on hydrogel lenses.

METHODS

A study of protein adsorption on three commercial hydrogel contact lenses of different materials, Etafilcon A (2-hydroxyethyl methacrylate [HEMA] polymer with sodium methacrylate and 2-ethyl-2-hydroxymethyl-1,3-propanediol trimethacrylate), tefilcon (poly[HEMA] cross-linked and copolymerized with ethylene glycol dimethacrylate), and vifilcon A (methacrylic acid polymer with ethylene glycol dimethacrylate, HEMA and N-vinyl pyrrolidone) was undertaken by using a single protein solution, human serum albumin (HSA), and a radiolabel-tracer technique.

RESULTS

Static adsorption leading to multilayer adsorption was observed. Complete reversibility for adsorbed HSA on lenses did not exist. Some was tightly bound, whereas most was loosely bound and could be removed easily by rinsing in phosphate-buffered saline. Irreversible adsorption of HSA on the lenses was found to be time dependent and did not reach a maximum value even after 48 hours of adsorption. The amount of HSA adsorbed on the lenses-irreversibly as well as totally adsorbed protein-was in the order of vifilcon A > tefilcon > etafilcon A. Adsorption of HSA on the lenses increases with decreasing pH (range, 7.4 to 4) but always follows the above trend with respect to the different types of lenses.

CONCLUSIONS

Irreversible binding of HSA on lenses is governed by the kinetics of protein denaturation. Electrostatic interactions may not play a major role in HSA adsorption on hydrogel lenses. Some other factors, such as hydrophobic dehydration, and special monomer units, such as N-vinyl pyrrolidone in the lens materials, may favor adsorption of HSA.