Thioflavine-T and Congo Red reveal the polymorphism of insulin amyloid fibrils when probed by polarization-resolved fluorescence microscopy. - Archive ouverte HAL
Article Dans Une Revue Journal of Physical Chemistry B Année : 2013

Thioflavine-T and Congo Red reveal the polymorphism of insulin amyloid fibrils when probed by polarization-resolved fluorescence microscopy.

Julien Duboisset
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Patrick Ferrand
Wei He
Xiao Wang
  • Fonction : Auteur
Hervé Rigneault
Sophie Brasselet

Résumé

Amyloid fibrils are protein misfolding structures that involve a β-sheet structure and are associated with the pathologies of various neurodegenerative diseases. Here we show that Thioflavine-T and Congo Red, two major dyes used to image fibrils by fluorescence assays, can provide deep structural information when probed by means of polarization-resolved fluorescence microscopy. Unlike fluorescence anisotropy or fluorescence detected linear dichroism imaging, this technique allows to retrieve simultaneously both mean orientation and orientation dispersion of the dye, used here as a reporter of the fibril structure. We have observed that insulin amyloid fibrils exhibit a homogeneous behavior over the fibrils' length, confirming their structural uniformity. In addition, these results reveal the existence of various structures among the observed fibrils' population, in spite of a similar aspect when imaged with conventional fluorescence microscopy. This optical nondestructive technique opens perspectives for in vivo structural analyses or high throughput screening.
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Dates et versions

hal-00803617 , version 1 (08-10-2014)

Identifiants

Citer

Julien Duboisset, Patrick Ferrand, Wei He, Xiao Wang, Hervé Rigneault, et al.. Thioflavine-T and Congo Red reveal the polymorphism of insulin amyloid fibrils when probed by polarization-resolved fluorescence microscopy.. Journal of Physical Chemistry B, 2013, 117 (3), pp.784-8. ⟨10.1021/jp309528f⟩. ⟨hal-00803617⟩
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