Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 101, Issue 40, Pages 14420-14424Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0405933101
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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 mum but ranging from 10 to 150 mum. 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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