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- Title
Polymorphism of Amyloid Fibrils In Vivo.
- Authors
Annamalai, Karthikeyan; Gührs, Karl-Heinz; Koehler, Rolf; Schmidt, Matthias; Michel, Henri; Loos, Cornelia; Gaffney, Patricia M.; Sigurdson, Christina J.; Hegenbart, Ute; Schönland, Stefan; Fändrich, Marcus
- Abstract
Polymorphism is a wide-spread feature of amyloid-like fibrils formed in vitro, but it has so far remained unclear whether the fibrils formed within a patient are also affected by this phenomenon. In this study we show that the amyloid fibrils within a diseased individual can vary considerably in their three-dimensional architecture. We demonstrate this heterogeneity with amyloid fibrils deposited within different organs, formed from sequentially non-homologous polypeptide chains and affecting human or animals. Irrespective of amyloid type or source, we found in vivo fibrils to be polymorphic. These data imply that the chemical principles of fibril assembly that lead to such polymorphism are fundamentally conserved in vivo and in vitro.
- Subjects
IN vivo studies; AMYLOID; POLYPEPTIDES; PARKINSON'S disease; GENETIC polymorphisms; IN vitro studies
- Publication
Angewandte Chemie International Edition, 2016, Vol 55, Issue 15, p4822
- ISSN
1433-7851
- Publication type
Article
- DOI
10.1002/anie.201511524