Abstract
The α-chymotrypsin is widely present in the digestive system of prokaryotes and eukaryotes that helps in the digestion by the hydrolysis of the peptide bond. It is serine protease enzyme (E.C. 3.4.21.1) and involves in many biological processes as well as in pancreatic disorders. In the previous study, marine red alga namely Jolyna laminariodes was used for the isolation of succinylanthranilic acid ester (2). Further, analogues were synthesised from anthranilic acid by using succinic anhydride, maleic anhydride and glutaric anhydride into corresponding dicarboxylic acids and further into acid ester including succinylanthranilic acid (1), succinylanthranilic acid ester (2), maleinylanthranilic acid (3), maleinylanthranilic acid ester (4), glutarnylanthranilic acid (5) and glutarnylanthranilic acid ester (6). For all natural products analogues percent inhibition against α-chymotrypsin have been calculated. In this study, molecular docking is used to estimate the binding energy of natural product analogues against α-chymotrypsin enzyme. The docking energies are in good agreement with experimental findings.
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