兔朊蛋白与人、鼠朊蛋白结构稳定性的计算研究
Computational Studies of the Structural Stability of Rabbit Prion Protein Compared to Human and Mouse Prion Proteins
摘要：
朊病毒疾病是影响人类和动物的致命性和高度传染性的神经退行性疾病。神经退行性疾病如克雅氏病、变异型克雅氏病、Gerstmann-Str $\ddot{a}$ ussler-Scheinker综合征、致死性家族性传染病、人类库鲁病、绵羊瘙痒病、牛海绵状脑病（或“疯牛病”）和牛慢性消耗病等都属于朊病毒病。目前还没有有效的治疗方法来治疗所有这些朊病毒疾病。据报道，狗、兔子和马对朊病毒疾病有抵抗力。到2010年底，所有狗、兔和马朊病毒蛋白的NMR结构（包括兔的X射线结构）都已完成，并已发布到蛋白质数据库中。因此，研究马、狗和兔朊蛋白的核磁共振和X-射线分子结构，对了解它们的免疫性朊蛋白疾病具有重要意义。作者发现狗和马的朊蛋白无论在中性还是低pH环境下都具有稳定的分子动力学结构，而兔朊蛋白只有在中性pH环境下才具有稳定的分子动力学结构。在低pH环境下，兔朊蛋白稳定的$α$ -螺旋分子结构塌缩成$β$ -折叠结构。本文重点研究了兔朊蛋白（在其C-末端NMR、同源性和X-射线分子结构区域RaPrP $^\text{C}$（120-230）），并与人和小鼠朊蛋白（分别为HuPrP $^\text{C}$（125-228）和MoPrP $^\text{C}$（124-226））进行比较。作者发现，在中性pH环境下，一些盐桥有助于兔朊蛋白的结构稳定性。
英文摘要：
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases affecting humans and animals. The neurodegenerative diseases such as Creutzfeldt-Jakob disease, variant Creutzfeldt-Jakob diseases, Gerstmann-Str$\ddot{a}$ussler-Scheinker syndrome, Fatal Familial Insomnia, Kuru in humans, scrapie in sheep, bovine spongiform encephalopathy (or 'mad-cow' disease) and chronic wasting disease in cattle belong to prion diseases. By now there have not been some effective therapeutic approaches to treat all these prion diseases. Dogs, rabbits and horses were reported to be resistant to prion diseases. By the end of year 2010 all the NMR structures of dog, rabbit and horse prion proteins (X-ray for rabbits too) had been finished to release into protein data bank. Thus, at this moment it is very worth studying the NMR and X-ray molecular structures of horse, dog and rabbit prion proteins to obtain insights into their immunity prion diseases. The author found that dog and horse prion proteins have stable molecular dynamical structures whether under neutral or low pH environments, but rabbit prion protein has stable molecular dynamical structures only under neutral pH environment. Under low pH environment, the stable $α$-helical molecular structures of rabbit prion protein collapse into $β$-sheet structures. This article focuses the studies on rabbit prion protein (within its C-terminal NMR, Homology and X-ray molecular structured region RaPrP$^\text{C}$ (120-230)), compared with human and mouse prion proteins (HuPrP$^\text{C}$ (125-228) and MoPrP$^\text{C}$ (124-226) respectively). The author finds that some salt bridges contribute to the structural stability of rabbit prion protein under neutral pH environment.
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