Related Experiment Video
Updated: May 23, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Formation of amyloid fibrils from β-amylase
Jian-Chau Luo1, Shing-Chuen Wang, Wei-Bang Jian
1Department of Life Science, National Chung Cheng University, Ming-Hsiung, Chia-Yi, Taiwan.
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.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Organization
