The age-dependent loss of solubility and aggregation of crystallins constitute the pathological hallmarks of cataract. Several biochemical and biophysical factors are responsible for the reduction of crystallins’ solubility and formation of irreversible protein aggregates, which display amyloid-like characteristics. The present study reports the heat-induced aggregation of soluble proteins isolated from human cataract lenses and the formation of amyloid-like structures. Exposure of protein at 55 °C for 4 h resulted in extensive (≈ 60%) protein aggregation. The heat-induced protein aggregates displayed substantial (≈ 20 nm) redshift in the wavelength of maximum absorption (λ_max) of Congo red (CR) and increase in Thioflavin T (ThT) fluorescence emission intensity, indicating the presence of amyloid-like structures in the heat-induced protein aggregates. Subsequently, the addition of trehalose resulted in substantial inhibition of heat-induced aggregation and the formation of amyloid-like structure. The ability of trehalose to inhibit the heat-induced aggregation was found to be linearly dependent upon its concentration used. The optimum effect was observed in the presence of 30–40% (w/v) trehalose where the aggregated was found to be reduced from 60 to 30%. The present study demonstrated the ability to trehalose to inhibit the protein aggregation and interfere with the formation of amyloid-like structures.

年龄依赖性的溶解度损失和结晶蛋白的聚集构成白内障的病理学特征。几种生物化学和生物物理因素是导致结晶蛋白溶解度降低和不可逆蛋白质聚集体形成的原因，蛋白质聚集体具有淀粉样蛋白样特征。本研究报道了从人白内障晶状体分离的可溶性蛋白质的热诱导聚集和淀粉样结构的形成。蛋白质在55°C下暴露4 h导致蛋白质广泛聚集（≈60％）。热诱导的蛋白质聚集体在最大吸收波长（_λmax刚果红（CR）和硫黄素T（ThT）荧光发射强度的增加，表明在热诱导的蛋白质聚集体中存在淀粉样蛋白样结构。随后，海藻糖的加入导致热诱导的聚集的实质性抑制和淀粉样结构的形成。发现海藻糖抑制热诱导的聚集的能力线性依赖于其使用的浓度。在存在30–40％（w / v）海藻糖的情况下观察到最佳效果，发现其中的聚集体从60％降至30％。本研究证明了海藻糖抑制蛋白质聚集和干扰淀粉样结构形成的能力。