Значения термина thioflavin t на английском

The amyloid-like property of the nanofibrils was confirmed via thioflavin T staining and atomic force microscopy.

Interestingly, changes in the fluorescence excitation and emission of thioflavin T were also dependent on the micelle formation.

Our data suggests that the micelles of thioflavin T bind amyloid fibrils leading to enhancement of fluorescence emission.

As shown by thioflavin T fluorescence monitoring, the formation of this cross-link accelerated the aggregation of native alpha-synuclein.

A tridecapeptide containing this sequence formed fibers that bound Congo red and thioflavin T and had characteristic amyloid morphology.

Increasing concentration of thioflavin T above the critical micellar concentration shows increased numbers of micelles bound along the length of the amyloid fibrils.

This suggests that positive charge on the thioflavin T molecule has a role in its micelle formation that then bind the amyloid fibrils.

We find, using thioflavin T fluorescence and electron microscopy assays, that 30 of the molecules inhibit the aggregation process, whereas 36 activate fibril formation.

In aqueous solutions, thioflavin T was found to exist as micelles at concentrations commonly used to monitor fibrils by fluorescence assay (approximately 10-20 microM).