Interaction of α-synuclein with Rhus typhina tannin – Implication for Parkinson’s disease
Szymon Sekowski, Maksim Ionov, Nodira Abdulladjanova, Rustam Makhmudov, Saidmukhtar Mavlyanov, Katarzyna Milowska, Maria Bryszewska, Maria Zamaraeva
Colloids and Surfaces B: Biointerfaces
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.
Circular dichroism, Secondary structure, Chemical stability, Aggregation, Biochemistry