Chaudhury Susmitnarayan, Roy Pritam, Dasgupta Swagata
Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
Department of Chemistry, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
Biochimie. 2017 Jun;137:46-55. doi: 10.1016/j.biochi.2017.02.016. Epub 2017 Mar 8.
Age related cataract is a major cause of visual loss worldwide that is a result of opacification of the eye lens proteins. One of the major reasons behind this deterioration is UV induced oxidative damage. The study reported here is focused on an investigation of the oxidative stress induced damage to γB-crystallin under UV exposure. Human γB-crystallin has been expressed and purified from E. coli. We have found that epicatechin gallate (ECG) has a higher affinity towards the protein compared to epigallocatechin (EGC). The in vitro study of UV irradiation under oxidative damage to the protein in the presence of increasing concentrations of GTPs is indicative of their effective role as potent inhibitors of oxidative damage. Docking analyses show that the GTPs bind to the cleft between the domains of human γB-crystallin that may be associated with the protection of the protein from oxidative damage.
年龄相关性白内障是全球视力丧失的主要原因，它是由眼晶状体蛋白混浊所致。这种退变背后的主要原因之一是紫外线诱导的氧化损伤。此处报道的研究聚焦于紫外线照射下氧化应激对γB-晶状体蛋白的损伤研究。人γB-晶状体蛋白已从大肠杆菌中表达并纯化出来。我们发现，与表没食子儿茶素（EGC）相比，表没食子儿茶素没食子酸酯（ECG）对该蛋白具有更高的亲和力。在存在浓度不断增加的鸟苷三磷酸（GTPs）的情况下，对该蛋白氧化损伤时紫外线照射的体外研究表明，它们作为氧化损伤的有效抑制剂发挥了作用。对接分析表明，GTPs与人γB-晶状体蛋白结构域之间的裂隙结合，这可能与保护该蛋白免受氧化损伤有关。
