Diagnostics for amyloid fibril formation: where to begin?
Danny M Hatters1, Michael D W Griffin
1Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC, Australia. dhatters@unimelb.edu.au
Methods in Molecular Biology (Clifton, N.J.)
|June 30, 2011
Summary
This study explores how to identify amyloid-like fibrils in proteins, a property more common than previously thought. It details methods for measuring fibrillization kinetics and using dyes like Congo Red and thioflavin T.
Area of Science:
- Biochemistry
- Molecular Biology
- Biophysics
Background:
- While 25 proteins are linked to disease-associated amyloid fibrils in vivo, the capacity for amyloid-like fibril formation is a more widespread protein property.
- Understanding this fundamental property offers insights into protein folding and misfolding thermodynamics.
Purpose of the Study:
- To outline basic steps for defining amyloid-like properties of a protein.
- To describe methods for measuring the kinetics of protein fibrillization.
Main Methods:
- Discusses fundamental tests for protein aggregation.
- Details the use of amyloid-reactive dyes, specifically Congo Red and thioflavin T, for detecting fibril presence.
Main Results:
- Provides a framework for identifying and characterizing amyloid-like fibril formation in proteins.
- Highlights the utility of Congo Red and thioflavin T assays as key indicators.
Conclusions:
- The ability to form amyloid-like fibrils is a common protein characteristic beyond disease association.
- Standardized methods and dye-based assays are crucial for studying protein fibrillization kinetics and thermodynamics.
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Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
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Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called 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 deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...