期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 55, 期 15, 页码 4822-4825出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201511524
关键词
Alzheimer's disease; Parkinson's disease; prions; protein folding; systemic amyloidosis
资金
- Bundesministerium fur Forschung and Bildung (BMBF, GERAMY network on systemic AL amyloidosis in Germany) [FKZ 01GM110]
- Deutsche Forschungsgemeinschaft [FA 456/15-1]
- Department of Cardiology, University Hospital Heidelberg
- Department of Cardio-Surgery, University Hospital Heidelberg
Polymorphism is a wide-spread feature of amyloid-like fibrils formed invitro, 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 invivo fibrils to be polymorphic. These data imply that the chemical principles of fibril assembly that lead to such polymorphism are fundamentally conserved invivo and invitro.
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