Title

Authors

Affiliation

¹Department of Studies in Physics, Manasagangotri, University of Mysore, Mysore- 570006, India; ²P. G. Department of Chemistry, Central College Campus, Bangalore University, Bangalore- 560001, India; ³Department of Physics, Acharya Institute of Technology, Bangalore- 560090, India

Email

mahendra@physics.uni-mysore.ac.in; *Corresponding author

Article Type

Hypothesis

Date

Received April 20, 2014; Accepted May 04, 2014; Published May 20, 2014

Protein kinases are important drug targets in human cancers, inflammation and metabolic diseases. Docking studies was performed for all the benzimidazopyrimidine and coumarin substituted benzimidazopyridimine derivatives with human Aurora A kinase target (3FDN) employing flexible ligand docking approach by using AutoDock 4.2. All the compounds were found to have minimum binding energy ranging from -6.26 to -9.29 kJ/mol. Among the molecules tested for docking study, 10-(6-Bromo-2-oxo-2H-chromen-4-ylmethyl)-2-isopropyl-10H-benzo[4,5]imidazo[1,2-a]pyrimidin-4-one (2k) showed minimum binding energy (-9.29 kJ/mol) with ligand efficiency of -0.31. All the ligands were docked deeply within the binding pocket region of 3FDN showing hydrogen bonds with Ala 213 and Asn 261. The docking study results showed that these derivatives are excellent inhibitor of human Aurora A kinase target; and also all these docked compounds have good inhibition constant, vdW + Hbond + desolv energy with best RMSD value.

Keywords

Benzimidazopyrimidine and coumarin substituted benzimidazopyridimine derivatives, Single crystal structure, Aurora A, Docking studies.

Citation

Chandra et al. Bioinformation 10(5):288-292 (2014)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

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.