Title |
Binding energy calculation of GSK-3 protein of human against some anti-diabetic compounds of Momordica charantia linn (Bitter melon) |
Authors |
Ridip Hazarika1*, Pratap Parida2, B Neog1 & RNS Yadav2 |
Affiliation |
1Department of Life Sciences, Dibrugarh University, Assam-786004, India; 2Bioinformatics Infrastructure Facility (BIF), Centre for Studies in Biotechnology, Dibrugarh University, Assam-786004, India
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ridiphaz@gmail.com; *Corresponding author
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Article Type |
Hypothesis
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Date |
Received February 13, 2012; Accepted March 08, 2012; Published March 31, 2012
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Abstract |
Diabetes is one of the major life threatening diseases worldwide. It creates major health problems in urban India. Glycogen Synthase Kinase-3 (GSK-3) protein of human is known for phosphorylating and inactivating glycogen synthase which also acts as a negative regulator in the hormonal control of glucose homeostasis. In traditional medicine, Momordica charantia is used as anti-diabetic plant because of its hypoglycemic effect. Hence to block the active site of the GSK-3 protein three anti-diabetic compounds namely, charantin, momordenol & momordicilin were taken from Momordica charantia for docking study and calculation of binding energy. The aim of present investigation is to find the binding energy of three major insulin-like active compounds against glycogen synthase kinase-3 (GSK-3), one of the key proteins involved in carbohydrate metabolism, with the help of molecular docking using ExomeTM Horizon suite. The study recorded minimum binding energy by momordicilin in comparison to the others.
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Keywords |
Anti-diabetic, Docking, ExomeTM Horizon suite, GSK-3, Momordica charantia
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Citation |
Hazarika et al.
Bioinformation 8(6): 251-254 (2012) |
Edited by |
P Kangueane
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ISSN |
0973-2063
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Publisher |
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License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |