The relationship between contact lens surface charge and in-vitro protein deposition levels.

Abstract

The adsorption of lysozyme and human serum albumin (HSA) onto hydrogel contact lenses was investigated as a function of lens surface charge. Anionic, cationic and non-ionic contact lenses were deposited using single protein solutions of identical pH and osmolarity. Protein deposition was analyzed using matrix assisted laser desorption ionization mass spectrometry (MALDI-ToF MS) and compared to a direct UV protein analysis method, the bicinchoninic acid (BCA) assay. The results showed remarkable consistency between the two techniques. By inference of results from analyses of sample solutions, lysozyme, a positively charged protein at physiological pH, was only detected on the anionic surface charged contact lenses, presumably a result of electrostatic interactions. Neither the cationic nor the non-ionic lenses deposited lysozyme, possibly due to charge repulsion. HSA, a negatively charged protein at physiological pH, was detected on the cationic lenses, again as a result of electrostatic interactions. The fact that HSA was not observed on either the anionic or non-ionic charged species further demonstrates the effect of charge repulsion.