کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2048482 1074082 2012 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Formation of amyloid fibrils from β-amylase
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Formation of amyloid fibrils from β-amylase
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 586, Issue 6, 23 March 2012, Pages 680–685
نویسندگان
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