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

By: RAGHAVENDRA, H. L.
Contributor(s): BHARATH, R.
Publisher: Mumbai Indian Journal of Pharmaceutical Science 2021Edition: Vol.83(2), March-April.Description: 271-277p.Subject(s): PHARMACEUTICSOnline resources: Click here In: Indian journal of pharmaceutical sciencesSummary: 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 enzymeα-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 ofRubus 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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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 enzymeα-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 ofRubus
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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