Hall Brad, Jones Lyndon W, Forrest James A
*PhD †PhD, FCOptom, FAAO Centre for Contact Lens Research, School of Optometry and Vision Science (all authors), and Department of Physics and Astronomy and Guelph-Waterloo Physics Institute (LWJ, JAF), University of Waterloo, Waterloo, Ontario, Canada.
Optom Vis Sci. 2015 Jul;92(7):781-9. doi: 10.1097/OPX.0000000000000618.
To compare the adsorption of lysozyme, lactoferrin, and albumin to various contact lens materials, between single-protein solutions and a multicomponent artificial tear solution (ATS). Additionally, extra steps were taken to distinguish loosely and tightly bound protein, the latter of which may be fully or partially denatured.
Using a previously described ATS, we measured the time-dependent adsorption of lys, lac, and alb onto one conventional hydrogel and four silicone hydrogel contact lens materials between the first minute and up to 1 week of protein interaction with the material surface. Proteins were quantified using I radiolabeling of each protein individually in ATS and buffered saline. Extra steps were taken to limit the amount of unbound I and to quantify the amount of reversibly bound protein.
Comfilcon A, balafilcon A, and etafilcon A did not show any relevant competitive adsorption between the ATS components and lys, lac, or alb until after 1 week. Competitive adsorption effects for lys, lac, and alb were observed in as little as 1 minute on lotrafilcon B. Lotrafilcon B had no reversibly bound protein at any time points. The ionic materials balafilcon A and etafilcon A deposited significant amounts of reversibly bound lysozyme and lactoferrin in just 10 minutes. Senofilcon A apparent deposition was below our thresholds of confidence for this protein quantification method.
Both the competition between lys, lac, and alb and ATS components and the reversibility of these bound proteins is material specific. Coadsorption of lys, lac, and alb with ATS components can increase the reversibility of their adsorption.
比较溶菌酶、乳铁蛋白和白蛋白在单蛋白溶液与多组分人工泪液溶液（ATS）中对各种隐形眼镜材料的吸附情况。此外，还采取了额外步骤来区分松散结合和紧密结合的蛋白质，后者可能会完全或部分变性。
使用先前描述的ATS，我们测量了溶菌酶、乳铁蛋白和白蛋白在与材料表面发生蛋白质相互作用的第一分钟至长达1周的时间内，在一种传统水凝胶和四种硅水凝胶隐形眼镜材料上随时间变化的吸附情况。在ATS和缓冲盐溶液中分别对每种蛋白质进行放射性标记来定量蛋白质。采取额外步骤来限制未结合放射性物质的量，并对可逆结合蛋白质的量进行定量。
直到1周后，Comfilcon A、balafilcon A和etafilcon A才在ATS成分与溶菌酶、乳铁蛋白或白蛋白之间显示出任何相关的竞争性吸附。在lotrafilcon B上，溶菌酶、乳铁蛋白和白蛋白在短短1分钟内就观察到了竞争性吸附效应。Lotrafilcon B在任何时间点都没有可逆结合的蛋白质。离子材料balafilcon A和etafilcon A在仅10分钟内就沉积了大量可逆结合的溶菌酶和乳铁蛋白。Senofilcon A的表观沉积量低于我们对这种蛋白质定量方法的置信阈值。
溶菌酶、乳铁蛋白和白蛋白与ATS成分之间的竞争以及这些结合蛋白质的可逆性都是材料特异性的。溶菌酶、乳铁蛋白和白蛋白与ATS成分的共吸附可以增加它们吸附的可逆性。
