Abstract
The aim of this study was to evaluate a new digestion method to quantify protein deposition on contact lenses. Four silicone hydrogel and one hydrogel contact lens material were incubated in lactoferrin, lysozyme, immunoglobulin A, and bovine serum albumin solutions at approximate physiological concentrations and temperature. Immobilized trypsin was used to digest the protein deposits from the contact lens surfaces. The total protein absorbed to lenses was extracted and digested using sequencing grade trypsin. The tryptic peptides were quantified using selected reaction monitoring mass spectrometry. The concentration of surface protein deposits was either lower than or the same as the total protein for all lens types and proteins. Immobilised trypsin can digest protein deposits from the surface of contact lenses. This ability to analyse the amount of protein at a contact lens surface may help in elucidating the effect of surface deposition on clinical outcomes during lens wear.
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