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Understanding Pharmacodynamics of Butyl Isobutyl Phthalate: Where In vitro and In silico Studies Converge

Author(s): H. L. Raghavendra*, B. R. Bharath, T. R. P. Kekuda, D. M. Chetan, M. M. V. N. L. Chaitanya and H. S. S. KUMAR
Department of Pharmacology, HSK College of Pharmacy, BVVS Campus, Bagalkot-587101, 1Department of Computational Biology, Atrimed Biotech LLP, Banglore-560100, 2Department of Microbiology, S.R.N.M.N College of Applied Sciences, Balraj Urs Road, Shivamogga-577201, 3Department of Biotechnology, NMAM Institute of Technology, Nitte, Karkala-574110, 4College of Medicine and Health Sciences, Department of Pharmacy (Pharmacognosy), Dilla University, Dilla, Ethiopia, 5Department of Biotechnology and Bioinformatics, Kuvempu University, Shankaragatta-577451, India

Correspondence Address:
H. L. RAGHAVENDRA, Department of Pharmacology, HSK College of Pharmacy, BVVS Campus, Bagalkot-587101, India, E-mail:

Recent epidemiological studies suggest that postprandial hyperglycemia is an independent risk factor for cardiovascular disease. A human’s high carbohydrate diet majorly consists of a high carbohydrate diet and α-glucosidase is a glucosidase located in the brush border of the small intestine is involved in glycosidic cleavage of starch at α-glycosidic bonds. α-glucosidase inhibitors are a unique class of anti-diabetic drugs particularly useful in individuals with a high carbohydrate diet. α-glucosidase inhibitors works by competitively inhibiting the enzyme α-glucosidase at the brush border of the small intestines, thus delaying the digestion of complex carbohydrate and intestinal absorption of glucose. Hence, in the present study, the α-glucosidase inhibition activity of butyl isobutyl phthalate isolated from chloroform fraction of Rubus steudneri leaves investigated and its possible mechanism of action ascertained in silico. The compound was found to exhibit concentration-dependent inhibition of α-glucosidase with half-maximal inhibitory concentration value of 10.68 g/ml. The results of in vitro α-glucosidase inhibition assay for butyl isobutyl phthalate were promising and substantiated by molecular docking and molecular dynamics studies.

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