Objective: The aim of this study is to evaluate the depolymerization effect of baicalein on mature fibrils of alpha-synuclein.

Background: The aggregation and oligomerization of alpha-synuclein (α-SN), a protein which is available at high concentration in the brain’s neuronal cells, is believed to play an important role in the pathology of Parkinson’s disease. There are several molecules which have the potential to inhibit aggregation but few could depolymerize mature fibrils. Baicalein, a small molecule derived from Scutellaria baicalensis Georgi, showed to have potential to inhibit fibrillation. Nevertheless, its low solubility and stability disrupt its function in the body fluid. Nowadays, using nanoparticles as candidates for drug delivery is welcome worldwide as they can unravel some problems regarding drugs characters like their high hydrophobicity, instability and low solubility in physiological fluids.

Method: Herein, we report on the potential of baicalein incorporated nanoliposome (NLP-Ba) to disaggregate/depolymerize α-SN aggregates in vitro. The protein was undertaken the fibrillation process and the adopted mature fibrils were exposed to NLP-Ba either without or with shaking. ThT fluorescence intensity and fast protein liquid chromatography (FPLC) were used to determine the disaggregates fibrils.

Results: NLP-Ba showed to have high potential to depolymerize fibrils by using ThT fluorescence intensity and FPLC. This result demonstrated that the potential of baicalein in the NLP could still be preserved.

Conclusion: This study could open a new avenue in using potential but unstable drug in neurodegenerative diseases including Parkinson’s disease. This abstract has already been presented in the “20th National Congress and the 8th International Congress on Biology” Maragheh Iran, August 22-24, 2018 as poster presentation.

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MDS Abstracts - https://www.mdsabstracts.org/abstract/baicalein-incorporated-nanoliposome-disaggregates-alpha-synuclein-fibrils/