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A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridge.

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Huvent, Isabelle | Kamah, Amina | Cantrelle, François-Xavier | Barois, Nicolas | Slomianny, Christian | Smet-Nocca, Caroline | Landrieu, Isabelle | Lippens, Guy

Edité par CCSD ; Elsevier -

International audience. We study the aggregation of a fragment of the neuronal protein Tau that contains part of the proline rich domain and of the microtubule binding repeats. When incubated at 37 °C with heparin, the fragment readily forms fibers as witnessed by Thioflavin T fluorescence. Electron microscopy and NMR spectroscopy show bundled ribbon like structures with most residues rigidly incorporated in the fibril. Without its cysteines, this fragment still forms fibers of a similar morphology, but with lesser Thioflavin T binding sites and more mobility for the C-terminal residues.

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