Formation of amyloid fibrils from β-amylase

被引：5

作者：

Luo, Jian-Chau ^{[1
]}

Wang, Shing-Chuen ^{[1
]}

Jian, Wei-Bang ^{[1
]}

Chen, Chien-Hsing ^{[2
]}

Tang, Jaw-Luen ^{[2
]}

Lee, Cheng-I ^{[1
]}

机构：

[1] Natl Chung Cheng Univ, Dept Life Sci, Chiayi 62102, Taiwan

[2] Natl Chung Cheng Univ, Dept Phys, Chiayi 62102, Taiwan

来源：

FEBS LETTERS | 2012年 / 586卷 / 06期

关键词：

Prion; beta-Amylase; Amyloid fibril; Congo red birefringence; TEM; PRION PROTEIN; IN-VITRO; COMMON MECHANISM; LYSOZYME; OLIGOMERS; DISEASES; IMPLIES; DOMAIN;

D O I：

10.1016/j.febslet.2012.01.062

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

引用

页码：680 / 685

页数：6

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