Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 117, Issue 3, Pages 784-788Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp309528f
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Funding
- Region Provence Alpes Cote d'Azur
- French Agence Nationale de la Recherche [ANR-2010-BLAN-150902]
- Erasmus Mundus scholarship [2010-2462/001-001/EMMC/Europhotonics]
- China Scholarship Council
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Amyloid fibrils are protein misfolding structures that involve a beta-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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