We conclude that Cyproheptadine hydrochloride, which was studied by docking experiments, exhibited the best inhibitory activity on salivary α-amylase in vitro & in silico. We conclude that Cyproheptadine hydrochloride, which was studied by docking experiments, exhibited the best inhibitory activity on salivary α-amylase in vitro & in silico.
This suggests that α-amylase inhibition is due to the synergistic effects of all peptides present in the sample. This result corroborates with those of Awosika and Aluko [ 22 ], who reported that unfractionated pea protein hydrolysates exhibited higher α-amylase inhibitory activity than their fractionated fractions.
Though, several classes of compounds and natural product libraries are better choices for in silico screening of drug targets, this is the first comprehensive study undertaken to analyze the constituents of α-amylase inhibition from a host plant and its endophyte simultaneously.
I%=ABSblank−ABStestABSblank∗100%, (1) where I(%) is the α-amylase inhibitory percentage. 2.3. Intestinal α-Glucosidase Inhibitory Method