Selectivity and localization of lysozyme uptake in contemporary hydrogel contact lens materials

TitleSelectivity and localization of lysozyme uptake in contemporary hydrogel contact lens materials
Publication TypeJournal Article
Year of Publication2017
AuthorsHeynen, M., B. N. Omali, Z. Fadli, C. Coles-Brennan, L. Subbaraman, and L. Jones
JournalJournal of Biomaterials Science, Polymer Edition
Volume28
Pagination1351-1364
Keywordsalbumin, Article, artificial tear, Asymmetric distribution, chemistry, confocal laser scanning microscopy, confocal microscopy, contact lens, Contact lenses, controlled study, Deposition, drug carrier, Drug Carriers, drug distribution, Enzymes, etafilcon a, hydrogel, Hydrogel contact lens, Hydrogels, Hydrophilic, hydrophilic contact lens, incubation time, lactoferrin, lysozyme, metabolism, Muramidase, nelfilcon a, nesofilcon A, ocufilcon b, omafilcon a, Polyethylene Glycol Dimethacrylate, polyethylene glycol dimethacrylate hydrogel, polymacon, polymer, priority journal, protein localization, protein transport, Proteins, radiolabel, silicone hydrogel, Silicone hydrogels, Silicones, Symmetric distributions, unclassified drug
Abstract

The purpose of this study was to investigate the early and selective uptake of lysozyme and the location of deposited lysozyme on contemporary hydrogel contact lens (CL) materials after exposure to an artificial tear solution (ATS) for 16 h. Seven different hydrogel CL materials [polymacon, omafilcon A, nelfilcon A, nesofilcon A, ocufilcon B, etafilcon A (Acuvue Moist), and etafilcon A (Acuvue Define)] were incubated in an ATS for various times. Total protein deposition was determined using a modified Bradford technique. Lysozyme, lactoferrin, and albumin deposition on CLs were determined using 125I-radiolabeling method. A confocal laser scanning microscopy (CLSM) technique was utilized to map the location of lysozyme uptake in an asymmetric environment. All lens materials had significant amounts of lysozyme after 1 min of exposure to ATS. After 16 h of incubation, higher levels of total protein deposited on the two etafilcon A-based lenses (Moist and Define), followed by ocufilcon B and both were significantly higher than all other CLs tested (p = 0.0001). The two etafilcon A materials (Moist and Define) also deposited the highest amounts of lysozyme (514.8 ± 28.4 and 527.1 ± 14.7 μg/lens respectively) when compared to other test CLs (p = 0.0001). The CLSM technique revealed that the non-ionic CLs tended to have symmetric distribution of lysozyme throughout the lens materials, while the ionic CLs had an asymmetric distribution, with the highest concentration of lysozyme on and near the exposed surface. The quantity and nature of proteins deposited on CLs varies, depending upon the chemical composition of the material. Among the various lenses tested, etafilcon A deposited the highest amount of total protein, most of it represented by lysozyme, which was largely located near the surface of the lens. © 2017 Informa UK Limited, trading as Taylor & Francis Group.

DOI10.1080/09205063.2017.1327751