Siddiqui Azad A, Sohail Aamir, Bhat Sheraz A, Rehman Md T, Bano Bilqees
Department of Biochemistry, Faculty of Life Sciences, AMU, Aligarh, U.P.202002, India.
Protein Pept Lett. 2015;22(5):449-59. doi: 10.2174/0929866522666150326105704.
The non-enzymatic reaction between proteins and reducing sugars, known as glycation, leads to the formation of inter and intramolecular cross-links of proteins. Stable end products called as advanced Maillard products or advanced glycation end products (AGEs) have received tremendous attention since last decades. It was suggested that the formation of AGEs not only modify the conformation of proteins but also induces altered biological activity. In this study, cystatin purified from almond was incubated with three different sugars namely D-ribose, fructose and lactose to monitor the glycation process. Structural changes induced in cystatin on glycation were studied using UV-visible spectroscopy, fluorescence spectroscopy, CD and FTIR techniques. Glycated cystatin was found to migrate slower on electrophoresis as compared to control cystatin. Biological activity data of glycated cystatin showed that D-ribose was most effective in inducing conformational changes with maximum altered activity.
蛋白质与还原糖之间的非酶促反应，即糖基化作用，会导致蛋白质分子间和分子内交联的形成。称为晚期美拉德产物或晚期糖基化终产物（AGEs）的稳定终产物自过去几十年以来受到了极大关注。有人提出，AGEs的形成不仅会改变蛋白质的构象，还会诱导生物活性发生改变。在本研究中，将从杏仁中纯化的胱抑素与三种不同的糖，即D-核糖、果糖和乳糖一起孵育，以监测糖基化过程。使用紫外可见光谱、荧光光谱、圆二色光谱和傅里叶变换红外光谱技术研究了胱抑素在糖基化过程中诱导的结构变化。结果发现，与对照胱抑素相比，糖基化胱抑素在电泳中迁移较慢。糖基化胱抑素的生物活性数据表明，D-核糖在诱导构象变化方面最有效，活性改变最大。
