Baicalein suppresses Repeat Tau fibrillization by sequestering oligomers

Alzheimer's disease (AD) is a neurodegenerative disorder caused by protein misfolding, aggregation and accumulation in the brain. A large number of molecules are being screened against these pathogenic proteins but the focus for therapeutics is shifting towards the natural compounds as aggregat...

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Bibliographic Details
Published in:Archives of biochemistry and biophysics 2019-10, Vol.675, p.108119-108119, Article 108119
Main Authors: Sonawane, Shweta Kishor, Balmik, Abhishek Ankur, Boral, Debjyoti, Ramasamy, Sureshkumar, Chinnathambi, Subashchandrabose
Format: Article
Language:English
Subjects:
Alzheimer disease
Alzheimer Disease - metabolism
Baicalein
Cell Line, Tumor
Flavanones - pharmacology
Humans
Microtubule assembly
Molecular Docking Simulation
Paired helical filaments
Protein aggregation
Tau protein
tau Proteins - metabolism
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Summary:Alzheimer's disease (AD) is a neurodegenerative disorder caused by protein misfolding, aggregation and accumulation in the brain. A large number of molecules are being screened against these pathogenic proteins but the focus for therapeutics is shifting towards the natural compounds as aggregation inhibitors, mainly due to their minimum adverse effects. Baicalein is a natural compound belonging to the class of flavonoids isolated from the Chinese herb Scutellaria baicalensis. Here we applied fluorescence, absorbance, microscopy, MALDI-TOF spectrophotometry and other biochemical techniques to investigate the interaction between Tau and Baicalein in vitro. We found the aggregation inhibitory properties of Baicalein for the repeat Tau. Overall, the potential of Baicalein in dissolving the preformed Tau oligomers as well as mature fibrils can be of utmost importance in therapeutics for Alzheimer's disease.
ISSN:0003-9861
1096-0384
DOI:10.1016/j.abb.2019.108119