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Amyloid fibrils: abnormal protein assembly.
Prion ( IF 1.9 ) Pub Date : 2008-07-20 , DOI: 10.4161/pri.2.3.7488
Roma N Rambaran 1 , Louise C Serpell
Affiliation  

Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs and tissues. Amyloid is insoluble and is structurally dominated by beta-sheet structure. Unlike other fibrous proteins it does not commonly have a structural, supportive or motility role but is associated with the pathology seen in a range of diseases known as the amyloidoses. These diseases include Alzheimer's, the spongiform encephalopathies and type II diabetes, all of which are progressive disorders with associated high morbidity and mortality. Not surprisingly, research into the physicochemical properties of amyloid and its formation is currently intensely pursued. In this chapter we will highlight the key scientific findings and discuss how the stability of amyloid fibrils impacts on bionanotechnology.

中文翻译:

淀粉样原纤维:蛋白质组装异常。

淀粉样蛋白是指在器官和组织中发现的异常纤维、细胞外、蛋白质沉积物。淀粉样蛋白是不溶性的,并且在结构上以β-折叠结构为主。与其他纤维蛋白不同,它通常不具有结构、支持或运动作用,但与一系列称为淀粉样变性的疾病中所见的病理学相关。这些疾病包括阿尔茨海默病、海绵状脑病和 II 型糖尿病,所有这些疾病都是进行性疾病,具有高发病率和死亡率。毫不奇怪,目前正在大力研究淀粉样蛋白的理化性质及其形成。在本章中,我们将重点介绍关键的科学发现,并讨论淀粉样原纤维的稳定性如何影响生物纳米技术。
更新日期:2019-11-01
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