Literature DB >> 22449963

Formation of amyloid fibrils from β-amylase.

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 Â
© 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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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


  3 in total

1.  Liberation of GPI-anchored prion from phospholipids accelerates amyloidogenic conversion.

Authors:  Shen-Jie Lin; Kun-Hua Yu; Jhih-Ru Wu; Chin-Fa Lee; Cheng-Ping Jheng; Hau-Ren Chen; Cheng-I Lee
Journal:  Int J Mol Sci       Date:  2013-09-03       Impact factor: 5.923

2.  Curcumin reduces amyloid fibrillation of prion protein and decreases reactive oxidative stress.

Authors:  Chi-Fen Lin; Kun-Hua Yu; Cheng-Ping Jheng; Raymond Chung; Cheng-I Lee
Journal:  Pathogens       Date:  2013-07-25

3.  The Effect of Octapeptide Repeats on Prion Folding and Misfolding.

Authors:  Kun-Hua Yu; Mei-Yu Huang; Yi-Ru Lee; Yu-Kie Lin; Hau-Ren Chen; Cheng-I Lee
Journal:  Int J Mol Sci       Date:  2021-02-11       Impact factor: 5.923

  3 in total

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