低温干燥过程中LEA蛋白对胰岛素结构稳定性的研究

来源 :生物医学工程学杂志 | 被引量 : 0次 | 上传用户:dotnetgroup
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当前蛋白药物日益在许多疾病的诊断、预防和治疗方面表现出重要的作用。然而,蛋白药物具有热敏性的特点,其活性结构大多不够稳定。因此,研究热敏性蛋白药物的有效保护方法并探究其保护机制对热敏蛋白药物的生产、贮存和应用具有重大的研究意义和实用价值。本文选择胰岛素为热敏性蛋白药物,胚胎发育晚期丰富(LEA)蛋白为活性保护剂,通过分子模拟方法详细研究了LEA蛋白对胰岛素生物活性的保护作用。研究结果表明:与没有任何保护的胰岛素的活性三维结构相比,LEA蛋白对胰岛素活性三维结构具有良好的保护作用,而且受保护的胰岛素的二级结构也非常稳定。由此可见,LEA蛋白是一个优良的热敏蛋白药物活性保护剂。 Current protein drugs are increasingly playing an important role in the diagnosis, prevention and treatment of many diseases. However, protein drugs are thermosensitive and most of their active structures are not stable enough. Therefore, it is of great research significance and practical value to study the effective protection methods of thermosensitive protein drugs and to explore their protection mechanism for the production, storage and application of thermosensitive protein drugs. In this paper, insulin as heat-sensitive protein drugs, late embryonic development enriched (LEA) protein as the active protective agent, through molecular simulation method to study in detail the protective effect of LEA protein on insulin biological activity. The results showed that compared with the active three-dimensional structure of insulin without any protection, LEA protein has a good protective effect on the three-dimensional structure of insulin activity, and the secondary structure of the protected insulin is also very stable. Thus, LEA protein is an excellent thermoprotein active pharmaceutical protective agent.
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