| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2048482 | FEBS Letters | 2012 | 6 Pages |
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.Structured summary of protein interactionsBeta-Amylase and Beta-Amylasebind by fluorescence technology (View Interaction: 1, 2) MoPrP and MoPrPbind by circular dichroism (View interaction) MoPrP and MoPrPbind by transmission electron microscopy (View interaction) Beta-Amylase and Beta-Amylasebind by circular dichroism (View interaction) MoPrP and MoPrPbind by fluorescence technology (View Interaction: 1, 2) Beta-Amylase and Beta-Amylasebind by transmission electron microscopy (View interaction)
►β-Amylase converts to amyloid fibrils, though β-amylase is not disease-related. ► Proteins with similar structure can form amyloid fibrils under the same conditions. ► The formation of amyloid fibrils is not necessarily disease-associated.
