| Literature DB >> 22449963 |
Jian-Chau Luo1, Shing-Chuen Wang, Wei-Bang Jian, Chien-Hsing Chen, Jaw-Luen Tang, Cheng-I Lee.
Abstract
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 ÂEntities:
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Year: 2012 PMID: 22449963 DOI: 10.1016/j.febslet.2012.01.062
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124