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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 β-amylase, a non-amyloid protein rich in α-helical structure, because the secondary structure of β-amylase is similar to that of prions. With the conditions for the fibril formation of prions, β-amylase proteins were converted into amyloid fibrils. The features of β-amylase proteins and fibrils are compared to prion proteins and fibrils. Furthermore, the cause of neurotoxicity in amyloid diseases is discussed. Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.


Jian-Chau Luo, Shing-Chuen Wang, Wei-Bang Jian, Chien-Hsing Chen, Jaw-Luen Tang, Cheng-I Lee. Formation of amyloid fibrils from β-amylase. FEBS letters. 2012 Mar 23;586(6):680-5

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PMID: 22449963

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