@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}
}
@article {47069,
	title = {Baicalein inhibits heparin-induced Tau aggregation by initializing non-toxic Tau oligomer formation},
	journal = {Cell Communication and Signaling},
	volume = {19},
	year = {2021},
	month = {FEB },
	pages = {16},
	type = {Article},
	abstract = {<p>Background: Amyloid aggregate deposition is the key feature of Alzheimer{\textquoteright}s disease. The proteinaceous aggregates found in the afflicted brain are the intra-neuronal neurofibrillary tangles formed by the microtubule-associated protein Tau and extracellular deposits, senile plaques, of amyloid beta (A beta) peptide proteolytically derived from the amyloid precursor protein. Accumulation of these aggregates has manifestations in the later stages of the disease, such as memory loss and cognitive inabilities originating from the neuronal dysfunction, neurodegeneration, and brain atrophy. Treatment of this disease at the late stages is difficult, and many clinical trials have failed. Hence, the goal is to find means capable of preventing the aggregation of these intrinsically disordered proteins by inhibiting the early stages of their pathological transformations. Polyphenols are known to be neuroprotective agents with the noticeable potential against many neurodegenerative diseases, such as Alzheimer{\textquoteright}s, Parkinson{\textquoteright}s, and Prion diseases. Methods: We analyzed the capability of Baicalein to inhibit aggregation of human Tau protein by a multifactorial analysis that included several biophysical and biochemical techniques. Results: The potency of Baicalein, a polyphenol from the Scutellaria baicalensis Georgi, against in vitro Tau aggregation and PHF dissolution has been screened and validated. ThS fluorescence assay revealed the potent inhibitory activity of Baicalein, whereas ANS revealed its mechanism of Tau inhibition viz. by oligomer capture and dissociation. In addition, Baicalein dissolved the preformed mature fibrils of Tau thereby possessing a dual target action. Tau oligomers formed by Baicalein were non-toxic to neuronal cells, highlighting its role as a potent molecule to be screened against AD. Conclusion: In conclusion, Baicalein inhibits aggregation of hTau40 by enhancing the formation of SDS-stable oligomers and preventing fibril formation. Baicalein-induced oligomers do not affect the viability of the neuroblastoma cells. Therefore, Baicalein can be considered as a lead molecule against Tau pathology in AD.</p>
},
	keywords = {Alzheimer{\textquoteright}s disease, Baicalein, Tau dissolution, Tau inhibition, Tau Oligomers},
	doi = {10.1186/s12964-021-00704-3},
	author = {Sonawane, Shweta Kishor and Uversky, Vladimir N. and Chinnathambi, Subashchandrabose}
}
