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In silico molecular docking on bioactive compounds from indian medicinal plants against type 2 diabetic target proteins: a computational approach

By: Thamaraiselvi, L.
Contributor(s): Selvankumar, T.
Publisher: Mumbai Indian Journal of Pharmaceutical Science 2021Edition: Vol.83(6), Nov-Dec.Description: 1273-1279p.Subject(s): PHARMACEUTICSOnline resources: Clic here In: Indian journal of pharmaceutical sciencesSummary: Natural chemical compounds from medicinal plants used for the healing of diseases and disorders with fewer side effects, easy accessibility and economically cheap. The current study was aimed at finding novel drug like molecules as anti-diabetic compounds using in silico approach. Intermolecular interactions between target proteins and different antidiabetic compounds were observed. Five phytocompounds were selected from Plumbago zeylanica, Neolitsea cassia and Wrightia tinctoria and taken for molecular docking against human pancreatic alpha-amylase and human dipeptidyl peptidase IV using Autodock 4.2. Among the five phyto compounds, 6 urs-12-en-24-oic acid Plumbago zeylanica is the best compound for both the human pancreatic alpha-amylase and human dipeptidyl peptidase IV inhibition, as it possessed higher value in molecular dockings.
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Natural chemical compounds from medicinal plants used for the healing of diseases and disorders with
fewer side effects, easy accessibility and economically cheap. The current study was aimed at finding novel
drug like molecules as anti-diabetic compounds using in silico approach. Intermolecular interactions
between target proteins and different antidiabetic compounds were observed. Five phytocompounds were
selected from Plumbago zeylanica, Neolitsea cassia and Wrightia tinctoria and taken for molecular docking
against human pancreatic alpha-amylase and human dipeptidyl peptidase IV using Autodock 4.2. Among
the five phyto compounds, 6 urs-12-en-24-oic acid Plumbago zeylanica is the best compound for both the
human pancreatic alpha-amylase and human dipeptidyl peptidase IV inhibition, as it possessed higher
value in molecular dockings.

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