Acetylcholine esterase inhibition activity of gloriosa superba and molecular docking study of its constituents against bacterial proteins

Abstract

Plant materials are invaluable sources in treatment of various diseases and research on certain plants has opened the way to development of various therapeutic agents. In the present study, the chloroform extract from the flowers of Gloriosa superba which belongs to the Colchicaceae family was subjected to column chromatography and it led to the isolation of myristyl alcohol which was identified by spectral methods. Eventhough G. superba exhibited a large number of biological activities, the acetylcholinesterase inhibition activity was not yet explored. The chloroform extract was studied for the acetylcholine esterase inhibition activity which showed an IC₅₀ value of 14µg/ml. This indicates that the chloroform extract of Gloriosa supera exhibits a strong AChE inhibition activity. Two compounds very often isolated from this genus colchinine and glorisine were subjected to molecular docking studies against the bacterial proteins 1UAG, 2X5O, 3UDI and 3TYE. It exhibited very good scores involving conventional H-bonding, alkyl, pi-alkyl and various other interactions.