纤维
淀粉样蛋白(真菌学)
电子显微镜
生物物理学
淀粉样纤维
化学
扫描电子显微镜
结晶学
材料科学
淀粉样β
生物
光学
病理
医学
无机化学
物理
疾病
复合材料
作者
Mark R.H. Krebs,Cait E. MacPhee,Aline F. Miller,Iain E. Dunlop,Christopher M. Dobson,Athene M. Donald
标识
DOI:10.1073/pnas.0405933101
摘要
Bovine insulin has long been known to self-assemble in vitro into amyloid fibrils. We have observed a further higher-order self-association of the protein into spherical structures, with diameters typically around 50 μm but ranging from 10 to 150 μm. In a polarizing light microscope, these structures exhibit a “Maltese-cross” extinction pattern typical of spherulites. Spherical structures of a similar size distribution can be observed in the environmental scanning electron microscope, which also reveals the presence of significant amounts of water in the structures. The spherulites contain a large quantity of well defined amyloid fibrils, suggesting that they are formed at least in part as a consequence of the self-assembly of preformed fibrils. Similar structures also have been observed in the tissues of patients suffering from amyloid disorders. The ability of amyloid fibrils to form such higher-order assemblies supports the hypothesis that they represent a generic form of polypeptide structure with properties that are analogous to those of classical synthetic polymers.
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