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Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status

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  • Published:
Journal of Chemical Biology

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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Acknowledgements

The Danish Medical Research Council, Novo Nordisk A/S, and the Drug Research Academy are thanked for financial support. The author thanks Bente Vestergaard and Per Hammarström for discussion and critical review of the manuscript.

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  1. Department of Pharmaceutics and Analytical Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Universitetsparken 2, 2100, Copenhagen, Denmark

    Minna Groenning

  2. IFM, Department of Chemistry, Linköping University, 581 83, Linköping, Sweden

    Minna Groenning

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Groenning, M. Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status. J Chem Biol 3, 1–18 (2010). https://doi.org/10.1007/s12154-009-0027-5

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