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[摘要]：Fibril formation has been considered a significant feature of amyloid proteins. However, it has been proposed that fibril formation is a common property of many proteins under appropriate conditions. We studied the fibril formation of beta-amylase, a non-amyloid protein rich in alpha-helical structure, because the secondary structure of beta-amylase is similar to that of prions. With the conditions for the fibril formation of prions, beta-amylase proteins were converted into amyloid fibrils. The features of beta-amylase proteins and fibrils are compared to prion proteins and fibrils. Furthermore, the cause of neurotoxicity in amyloid diseases is discussed. Structured summary of protein interactions: Beta-Amylase and Beta-Amylase bind by fluorescence technology (View Interaction: 1, 2) MoPrP and MoPrP bind by circular dichroism (View interaction) MoPrP and MoPrP bind by transmission electron microscopy (View interaction) Beta-Amylase and Beta-Amylase bind by circular dichroism (View interaction) MoPrP and MoPrP bind by fluorescence technology (View Interaction: 1, 2) Beta-Amylase and Beta-Amylase bind by transmission electron microscopy (View interaction) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
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