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Angew Chem Int Ed Engl. 2016 Apr 4;55(15):4822-5. doi: 10.1002/anie.201511524. Epub 2016 Mar 8.

Polymorphism of Amyloid Fibrils In Vivo.

Author information

1
Institute of Protein Biochemistry, Ulm University, Helmholtzstrasse 8/1, 89081, Ulm, Germany.
2
CF Protemics, Leibniz Institute on Aging-Fritz Lipmann Institute (FLI), Beutenbergstraße 11, 07745, Jena, Germany.
3
Institute of Human Genetics, Im Neuenheimer Feld 366, 69120, Heidelberg, Germany.
4
Department of Pathology, University of California, San Diego, 9500 Gilman Drive, MC 0162, La Jolla, CA, 92093-0612, USA.
5
Amyloidosis Center, Department of Internal Medicine V, Im Neuenheimer Feld 410, 69120, Heidelberg, Germany.
6
Institute of Protein Biochemistry, Ulm University, Helmholtzstrasse 8/1, 89081, Ulm, Germany. marcus.faendrich@uni-ulm.de.

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.

KEYWORDS:

Alzheimer's disease; Parkinson's disease; prions; protein folding; systemic amyloidosis

PMID:
26954430
PMCID:
PMC4864496
DOI:
10.1002/anie.201511524
[Indexed for MEDLINE]
Free PMC Article

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