作者: Karthikeyan Annamalai , Karl-Heinz Gührs , Rolf Koehler , Matthias Schmidt , Henri Michel
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摘要: Polymorphism is a wide-spread feature of amyloid-like fibrils formed in vitro, but it has so far remained unclear whether the within patient are also affected by this phenomenon. In study we show that amyloid diseased individual can vary considerably their three-dimensional architecture. We demonstrate heterogeneity with deposited different organs, from sequentially non-homologous polypeptide chains and affecting human or animals. Irrespective type source, found vivo to be polymorphic. These data imply chemical principles fibril assembly lead such polymorphism fundamentally conserved vitro.