Journal
COMPUTATIONAL BIOLOGY AND CHEMISTRY
Volume 64, Issue -, Pages 353-358Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.compbiolchem.2016.08.005
Keywords
Adenosine deaminase; Hibifolin; Molecular docking; Molecular dynamics; Isothermal titration calorimetry
Funding
- DBT, Government of India
- Kerala State Council for Science, Technology and Environment (KSCSTE)
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Adenosine deaminase (ADA) is an enzyme involved in purine metabolism. ADA converts adenosine to inosine and liberates ammonia. Because of their critical role in the differentiation and maturation of cells, the regulation of ADA activity is considered as a potential therapeutic approach to prevent malignant and inflammatory disorders. In the present study, the inhibitory activity of a plant flavonoid, hibifolin on ADA is investigated using enzyme kinetic assay and isothermal titration calorimetry. The inhibitory constant of hibifolin was found to be 49.92 mu M +/- 14 3.98 and the mode of binding was reversible. Isothermal titration calorimetry showed that the compound binds ADA with binding energy of -7.21 Kcal/mol. The in silica modeling and docking studies showed that the bound ligand is stabilized by hydrogen bonds with active site residues of the enzyme. The study reveals that hibifolin can act as a potential inhibitor of ADA. (C) 2016 Elsevier Ltd. All rights reserved.
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