Title
Interaction of α-synuclein with Rhus typhina tannin – Implication for Parkinson’s disease
Author
Szymon Sekowski, Maksim Ionov, Nodira Abdulladjanova, Rustam Makhmudov, Saidmukhtar Mavlyanov, Katarzyna Milowska, Maria Bryszewska, Maria Zamaraeva
Year
2017
Journal
Colloids and Surfaces B: Biointerfaces
Abstract
The etiology of Parkinson’s disease (PD) relates to α-synuclein, a small protein with the ability to aggregate and form Lewy bodies. One of its prevention strategies is inhibition of α-synuclein oligomerization. We have investigated the interaction of α-synuclein and human serum albumin with 3,6-bis-О-di-О-galloyl-1,2,4-tri-О-galloyl-β-D-glucose (a tannin isolated from the plant Rhus typhina). Using fluorescence spectroscopy method we found that this tannin interacts strongly with α-synuclein forming complexes. Circular dichroism analysis showed a time-dependent inhibition of α-synuclein aggregation in the presence of the tannin. On the other hand, 3,6-bis-О-di-О-galloyl-1,2,4-tri-О-galloyl-β-D-glucose had a much stronger interaction with human serum albumin than α-synuclein. The calculated binding constant for tannin-protein interaction was considerably higher for albumin than α-synuclein. This tannin interacted with albumin through a “sphere of action” mechanism. The results lead to the conclusion that 3,6-bis-О-di-О-galloyl-1,2,4-tri-О-galloyl-β-D-glucose is a potent preventive compound against Parkinson’s disease. However, this tannin interacts very strongly with human serum albumin, significantly reducing the bioavailability of this compound.
Instrument
J-815
Keywords
Circular dichroism, Secondary structure, Chemical stability, Aggregation, Biochemistry