@article {47164,
	title = {Baicalein suppresses repeat tau fibrillization by sequestering oligomers},
	journal = {Archives of Biochemistry and Biophysics},
	volume = {675},
	year = {2019},
	month = {OCT},
	pages = {108119},
	type = {Article},
	abstract = {<p>Alzheimer{\textquoteright}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{\textquoteright}s disease.</p>
},
	keywords = {Alzheimer disease, Baicalein, Microtubule assembly, Paired helical filaments, Protein aggregation, tau protein},
	issn = {0003-9861},
	doi = {10.1016/j.abb.2019.108119},
	author = {Sonawane, Shweta Kishor and Balmik, Abhishek Ankur and Boral, Debjyoti and Ramasamy, Sureshkumar and Chinnathambi, Subashchandrabose}
}
