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

作者：Huvent Isabelle; Kamah Amina; Cantrelle Francois Xavier; Barois Nicolas; Slomianny Christian; Smet Nocca Caroline; Landrieu Isabelle; Lippens Guy^*

来源：Biochemical and Biophysical Research Communications, 2014, 445(2): 299-303.

DOI：10.1016/j.bbrc.2014.01.161

• Tau
• Aggregation
• Nucleation
• Electron microscopy
• NMR spectroscopy

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 degrees 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.

• 出版日期2014-3-7