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Polymorphism of Amyloid Fibrils In Vivo.

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.

SUBMITTER: Annamalai K

PROVIDER: S-EPMC4864496 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature

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Polymorphism of Amyloid Fibrils In Vivo.

Annamalai Karthikeyan K Gührs Karl-Heinz KH Koehler Rolf R Schmidt Matthias M Michel Henri H Loos Cornelia C Gaffney Patricia M PM Sigurdson Christina J CJ Hegenbart Ute U Schönland Stefan S Fändrich Marcus M

Angewandte Chemie (International ed. in English) 20160308 15

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 hu ...[more]

PMID: 26954430

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