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Curr Opin Struct Biol. 2007 Feb;17(1):48-57. Epub 2007 Jan 23.

Polymorphism in the intermediates and products of amyloid assembly.

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Department of Structural Biology, University of Pittsburgh School of Medicine, 2046 Biomedical Sciences Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.


Amyloid formation reactions exhibit two classes of polymorphisms: the metastable intermediates commonly observed during amyloid formation and the range of conformationally distinct mature fibrils often seen at the reaction endpoint. Although recent data suggest that spherical oligomers and protofibrils in most cases are not obligate intermediates of amyloid assembly, oligomeric states might sometimes serve as on-pathway intermediates. Mature amyloid polymorphs self-propagate as a result of the normally very high fidelity of amyloid elongation, giving rise to strain behavior and species barriers in prion phenomena. Oligomers, protofibrils and various polymorphic forms of mature amyloid fibrils seem to be distinguished by differences in atomic structure that give rise to differences in observed morphologies.

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