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聚合材料的电离加速蛋白质在水凝胶隐形眼镜材料上的沉积。

The Ionization of Polymeric Materials Accelerates Protein Deposition on Hydrogel Contact Lens Material.

作者信息

Ahn Jihye, Choi Moonsung

机构信息

Department of Optometry, College of Energy and Biotechnology, Seoul National University of Science and Technology, Seoul 01811, Republic of Korea.

Convergence Institute of Biomedical Engineering and Biomaterials, Seoul National University of Science and Technology, Seoul 01811, Republic of Korea.

出版信息

Materials (Basel). 2023 Mar 6;16(5):2119. doi: 10.3390/ma16052119.

Abstract

Contact lens materials include polymers that are ionized in the ocular pH condition and are susceptible to protein deposition due to their surface characteristics. Herein, we investigated the effect of the electrostatic state of the contact lens material and protein on protein deposition level using hen egg white lysozyme (HEWL) and bovine serum albumin (BSA) as model proteins and etafilcon A and hilafilcon B as model contact lens materials. Only HEWL deposition on etafilcon A showed a statistically significant pH-dependency ( < 0.05); protein deposition increased with pH. HEWL showed a positive zeta potential at acidic pH, while BSA showed a negative zeta potential at basic pH. Only etafilcon A showed a statistically significant pH-dependent point of zero charge (PZC) ( < 0.05), implying that its surface charge became more negative under basic conditions. This pH-dependency of etafilcon A is attributed to the pH-responsive degree of ionization of its constituent methacrylic acid (MAA). The presence of MAA and its degree of ionization could accelerate protein deposition; more HEWL deposited as pH increased despite the weak positive surface charge of HEWL. The highly negatively charged etafilcon A surface attracted HEWL, even overwhelming weak positive charge of HEWL, increasing the deposition with pH.

摘要

隐形眼镜材料包括在眼内pH条件下会发生电离且因其表面特性易发生蛋白质沉积的聚合物。在此,我们以蛋清溶菌酶(HEWL)和牛血清白蛋白(BSA)作为模型蛋白,以依他氟康A和希拉氟康B作为模型隐形眼镜材料,研究了隐形眼镜材料和蛋白质的静电状态对蛋白质沉积水平的影响。仅HEWL在依他氟康A上的沉积表现出统计学上显著的pH依赖性(<0.05);蛋白质沉积随pH升高而增加。HEWL在酸性pH下显示正的ζ电位,而BSA在碱性pH下显示负的ζ电位。仅依他氟康A显示出统计学上显著的pH依赖性零电荷点(PZC)(<0.05),这意味着其表面电荷在碱性条件下变得更负。依他氟康A的这种pH依赖性归因于其组成甲基丙烯酸(MAA)的pH响应电离程度。MAA的存在及其电离程度可加速蛋白质沉积;尽管HEWL表面电荷呈弱正性,但随着pH升高,更多的HEWL沉积。带高度负电荷的依他氟康A表面吸引了HEWL,甚至超过了HEWL的弱正电荷,导致沉积随pH增加。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e21c/10004484/8d565448111c/materials-16-02119-g001.jpg

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