Comparative molecular docking studies of EGCG with SHaPrPC

Epigallocatechin gallate (EGCG) is a naturally occurring alkaloid found in green tea.It has been shown to bind with nanomolar affinity to the monomeric prion protein and induce conformational instability.A better understanding of the specific molecular interactions that impart this strong interaction and molecular rearrangement are of interest for the development of ligands that possess both high affinity yet impart stabilizing effects.Recently, it has been demonstrated that molecules with such characteristics reduce PrP sc titers in both in-vitro and ex-vivo experiments.To gain structural insights into EGCG's effect on the monomeric prion protein (PrP c ), comparative molecular docking studies of EGCG was performed against SHaPrP C using MOE, Sybyl and FlexX software docking programs.These results show that the side orientations of Tyr 169 and Tyr 218 play an important role in binding of EGCG near the amylome region motif between loop-2 and helix-2.