Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status |
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Authors: | Minna Groenning |
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Institution: | 1.Department of Pharmaceutics and Analytical Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Universitetsparken 2, 2100 Copenhagen, Denmark ;2.IFM, Department of Chemistry, Linköping University, 581 83 Linköping, Sweden |
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Abstract: | Because understanding amyloid fibrillation in molecular detail is essential for development of strategies to control amyloid
formation and overcome neurodegenerative disorders, increased understanding of present molecular probes as well as development
of new probes are of utmost importance. To date, the binding modes of these molecular probes to amyloid fibrils are by no
means adequately described or understood, and the large number of studies on Thioflavin T (ThT) and Congo Red (CR) binding
have resulted in models that are incomplete and conflicting. Different types of binding sites are likely to be present in
amyloid fibrils with differences in binding modes. ThT may bind in channels running parallel to the long axis of the fibril.
In the channels, ThT may bind in either a monomeric or dimeric form of which the molecular conformation is likely to be planar.
CR may bind in grooves formed along the β-sheets as a planar molecule in either a monomeric or supramolecular form. |
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Keywords: | Amyloid Binding mode Congo Red Fibrillation Molecular probes Thioflavin T |
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