The binding of thioflavin-T to amyloid fibrils: localisation and implications.
By M. Krebs, E. Bromley, A. Donald. Journal of Structural Biology, 2005
735 citations recorded by the source corpus.
Amyloid fibrils are a polymeric form of protein, involving a continuous beta-sheet with the strands perpendicular to the long axis of the fibril. Although typically implicated in diseases such as Alzheimer's disease and the transmissible spongiform encephalopathies, non disease-associated protein can also be converted into amyloid fibrils. Traditionally, amyloid fibrils are identified via the use of specific dyes such as Congo red and thioflavin-T, although their specificity is ill understood. Recently, solutions of bovine insulin and bovine beta-lactoglobulin have been found to form spherulites, micron-sized spherical structures containing radially arranged amyloid fibrils. When studied by confocal microscopy using polarised laser light and thioflavin-T, a consistent pattern of emission, rather than a uniform disc, was observed. This suggests the dye binds in a specific, regular fashion to amyloid fibrils. Confocal microscopy studies of thioflavin-T aligned in stretched poly-vinyl alcohol films showed that the dye dipole excitation axis lies parallel to the long molecular axis. Therefore, thioflavin-T binds to amyloid fibrils such that their long axes are parallel. We propose binding occurs in 'channels' that run along the length of the beta-sheet. Steric interactions between dye molecules and side chains indicate why thioflavin-T fluoresces more intensely when bound to amyloid fibrils and can explain why this interaction with amyloid fibrils is specific, but with varying efficiency.
Subfields: Clinical Biochemistry, Food Science, Physiology
View Paper: https://www.semanticscholar.org/paper/696acb8af943991bd2a4943b342fc64fb08bf03e
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Citations in the corpus
- Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation (2017, background): “It is commonly accepted that ThT binds to the side chain channels along the long axis of amyloid fibrils [6].”
- Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils (2010, background): “[38] revealed that ThTmolecules bound to fibrils are aligned parallel to the long axis of the fiber.”
- Functional Amyloid Formation within Mammalian Tissue (2005, background): “Recent studies have shown that thioflavin T binds in a regular fashion parallel to the amyloid fiber axis [31].”