The formation of spherulites by amyloid fibrils of bovine insulin

@article{citeulike:970310, abstract = {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 {micro}m but ranging from 10 to 150 {micro}m. 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. 10.1073/pnas.0405933101}, author = {Krebs, Mark R. and Macphee, Cait E. and Miller, Aline F. and Dunlop, Iain E. and Dobson, Christopher M. and Donald, Athene M. }, citeulike-article-id = {970310}, journal = {PNAS}, month = {October}, number = {40}, pages = {14420--14424}, posted-at = {2006-12-01 12:07:57}, priority = {2}, title = {The formation of spherulites by amyloid fibrils of bovine insulin}, url = {http://www.pnas.org/cgi/content/abstract/101/40/14420}, volume = {101}, year = {2004} }

TY - JOUR ID - citeulike:970310 L3 - citeulike-article-id:970310 TI - The formation of spherulites by amyloid fibrils of bovine insulin JF - PNAS VL - 101 IS - 40 SP - 14420 EP - 14424 N2 - 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 {micro}m but ranging from 10 to 150 {micro}m. 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. 10.1073/pnas.0405933101 AU - Krebs, Mark AU - Macphee, Cait AU - Miller, Aline AU - Dunlop, Iain AU - Dobson, Christopher AU - Donald, Athene PY - 2004/10/05/ UR - http://www.pnas.org/cgi/content/abstract/101/40/14420 ER -