The objective of the analysis is to determine the inhibitory function of α-amylase active compounds in Barleria prionitis L. Usage in studies of silico docking. In this respect the docking evaluation was for active plant constituent ligands. The standard inhibitor was acarbose, a known α-amylase inhibitor. The latest version of GLIDE Software v5.5 developed by Schrödinger has taken the place of silico docking studies. These results demonstrate that binding energy ranged from – 3.1 to -8.9 kcal/mol in all active components. If compared (-6.3 kcal/mol) to the norm. The inhibitors of α-amylase are excellent because of their structural parameters, as well as 1,8-dihydroxy-2,7-dimethyl 3,6-dimethoxy anthraquinone and Melilotic acid and Barlerin. Through these molecular docking studies, the effective α-amylase inhibitors for the treatment of diabetes are further developed.
