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Int. J. Mol. Sci. 2015, 16(3), 5180-5193; doi:10.3390/ijms16035180

Spectrofluorometric and Molecular Docking Studies on the Binding of Curcumenol and Curcumenone to Human Serum Albumin

1
Department of Chemistry, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia
2
Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia
3
Center of Natural products and Drug Discovery (CENAR), University of Malaya, 50603 Kuala Lumpur, Malaysia
4
Atta-ur-Rahman Institute for Natural Product Discovery, Universiti Teknologi MARA, Kampus Puncak Alam, 42300 Bandar Puncak Alam, Malaysia
*
Author to whom correspondence should be addressed.
Academic Editor: Jesus De Julián Ortiz
Received: 6 November 2014 / Revised: 6 January 2015 / Accepted: 9 January 2015 / Published: 6 March 2015
(This article belongs to the Section Physical Chemistry, Theoretical and Computational Chemistry)
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Abstract

Curcumenol and curcumenone are two major constituents of the plants of medicinally important genus of Curcuma, and often govern the pharmacological effect of these plant extracts. These two compounds, isolated from C. zedoaria rhizomes were studied for their binding to human serum albumin (HSA) using the fluorescence quench titration method. Molecular docking was also performed to get a more detailed insight into their interaction with HSA at the binding site. Additions of these sesquiterpenes to HSA produced significant fluorescence quenching and blue shifts in the emission spectra of HSA. Analysis of the fluorescence data pointed toward moderate binding affinity between the ligands and HSA, with curcumenone showing a relatively higher binding constant (2.46 × 105 M−1) in comparison to curcumenol (1.97 × 104 M−1). Cluster analyses revealed that site I is the preferred binding site for both molecules with a minimum binding energy of −6.77 kcal·mol−1. However, binding of these two molecules to site II cannot be ruled out as the binding energies were found to be −5.72 and −5.74 kcal·mol−1 for curcumenol and curcumenone, respectively. The interactions of both ligands with HSA involved hydrophobic interactions as well as hydrogen bonding. View Full-Text
Keywords: Curcuma zedoaria; sesquiterpene; human serum albumin; protein-ligand interaction; molecular docking; fluorescence spectroscopy Curcuma zedoaria; sesquiterpene; human serum albumin; protein-ligand interaction; molecular docking; fluorescence spectroscopy
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Hamdi, O.A.A.; Feroz, S.R.; Shilpi, J.A.; Anouar, E.H.; Mukarram, A.K.; Mohamad, S.B.; Tayyab, S.; Awang, K. Spectrofluorometric and Molecular Docking Studies on the Binding of Curcumenol and Curcumenone to Human Serum Albumin. Int. J. Mol. Sci. 2015, 16, 5180-5193.

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