Crystallins, which represent the major lens protein, play a significant role in ensuring the lens transparency and maintenance of appropriate refractive index of the lens that help in accurate focusing of incident visible light precisely on retina to create clear image perception. Aggregation of lens proteins is known to form the basis of cataract formation. The present study is an attempt to examine the stability of the lens protein aggregates, isolated from human cataract eye lens, against an anionic detergent Sodium dodecyl sulphate (SDS), which is known to disrupt the hydrophobic interaction of protein aggregates. Data that emerged from Congo red (CR), thioflavin T (ThT) and 8-anilino-1-naphthalene sulfonic acid (ANS) binding assay indicated their amyloidogenic nature. A significant reduction in the bathochromic shift of CR λmax and ThT fluorescence emission intensity were observed after treatment of the aggregated proteins with SDS. In the presence of SDS, a significant change in the number and size of the protein aggregates were observed during their morphological analyses under transmission electron microscopy (TEM). Based on the above data it became evident that the hydrophobic interaction plays a crucial role in formation and stabilizing the protein aggregates during cataract formation.

中文翻译：

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从人白内障晶状体中分离的淀粉样蛋白聚集体的分解

晶状体蛋白是主要的晶状体蛋白，在确保晶状体透明度和维持适当的晶状体折射率方面发挥着重要作用，有助于将入射可见光准确聚焦在视网膜上，从而产生清晰的图像感知。已知晶状体蛋白的聚集形成白内障形成的基础。本研究试图检查从人类白内障眼晶状体中分离出来的晶状体蛋白质聚集体对阴离子洗涤剂十二烷基硫酸钠 (SDS) 的稳定性，已知其会破坏蛋白质聚集体的疏水相互作用。来自刚果红 (CR)、硫代黄素 T (ThT) 和 8-anilino-1-萘磺酸 (ANS) 结合测定的数据表明它们的淀粉样蛋白性质。用 SDS 处理聚集的蛋白质后，观察到 CR λmax 和 ThT 荧光发射强度的红移显着降低。在存在 SDS 的情况下，在透射电子显微镜 (TEM) 下的形态分析过程中观察到蛋白质聚集体的数量和大小发生了显着变化。基于上述数据，很明显疏水相互作用在白内障形成过程中蛋白质聚集体的形成和稳定中起着至关重要的作用。