Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 675, Issue -, Pages -Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2019.108119
Keywords
Alzheimer disease; Tau protein; Protein aggregation; Paired helical filaments; Microtubule assembly; Baicalein
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Funding
- Department of Science and Technology-Science and Engineering Research Board [DST-SERB/EMR000306]
- CSIR-National Chemical Laboratory [MLP029526]
- Department of Biotechnology (DBT), India
- Shyama Prasad Mukherjee fellowship (SPMF) from Council of Scientific Industrial Research (CSIR), India
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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.
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