Department of Biotechnology, Indian Institute of Technology Guwahati, Guwahati 781039, Assam, India.
Biol Chem. 2009 Oct;390(10):1057-61. doi: 10.1515/BC.2009.107.
We identified a molten globule-like intermediate of 2,5-diketo-D-gluconate reductase A (DKGR) at pH 2.5, which has a prominent beta-sheet structure. The molten globule state of the protein shows amyloidogenic property >50 microm protein concentration. Interestingly, a 1:1 molar ratio of curcumin prevents amyloid formation as shown by the Thioflavin-T assay and atomic force microscopy. To the best of our knowledge, this is the first report on amyloid formation by an (alpha/beta)(8)-barrel protein. The results presented here indicate that the molten globule state has an important role in amyloid formation and potential application of curcumin in protein biotechnology as well as therapeutics against amyloid diseases.
我们在 pH 值为 2.5 时鉴定出 2,5-二酮-D-葡萄糖酸还原酶 A(DKGR)的类熔球中间体,其具有突出的β-折叠结构。该蛋白质的无定形状态 >50 微米蛋白浓度显示出淀粉样特性。有趣的是,姜黄素的 1:1 摩尔比可防止淀粉样形成,如噻唑蓝-T 测定和原子力显微镜所示。据我们所知,这是首次报道(α/β)(8)-桶蛋白的淀粉样形成。这里呈现的结果表明,无定形状态在淀粉样形成中具有重要作用,姜黄素在蛋白质生物技术以及抗淀粉样疾病的治疗中的潜在应用。