title: Inter-domain helix h10DOMI-h1DOMII is important in the molecular interaction of bovine serum albumin with curcumin: spectroscopic and computational analysis.
abstract: The importance of domain II in the molecular interaction of bovine serum albumin (BSA) with curcumin was investigated by fluorescence spectroscopy and molecular docking. At pH 7.4 BSA is in its native state. Domain III of BSA unfolds at pH 4.0, and domains I and III unfold in the presence of 5 M urea. Curcumin has a high quenching constant (K SV ~ 10(4) M (-1)) and moderate binding affinity (n ~ 0.5). The standard free energy change (∆G° ~ -25 kJ mol(-1)) indicates that binding is spontaneous. No significant change in ∆G° observed after unfolding of domain I or domain III. The standard change in enthalpy (∆H°) and entropy (∆S°) show that ionic and hydrophobic interactions are important in the binding. Computational studies revealed that the inter-domain helix h10DOMI-h1DOMII of BSA is the region of binding of curcumin, and residues Arg198 and Arg208 are important in binding. The binding site is located between sub-domains IB and IIA, and overlaps drug binding site-1.
authors: P.G. Department of Biotechnology, Utkal University, Bhubaneswar, India.
authors: Dhakaram
authors: D
authors: Pangeni
authors: Charu
authors: C
authors: Kapil
authors: Mohamad Aman
authors: MA
authors: Jairajpuri
authors: Priyankar
authors: P
authors: Sen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003474:Curcumin / Q000737:chemistry / Q000494:pharmacology*; D062105:Molecular Docking Simulation; D008969:Molecular Sequence Data; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism
chemical_list: D012710:Serum Albumin, Bovine; D003474:Curcumin
references: Biochemistry. 1981 May 26;20(11):3096-102
references: 7248271
references: FEBS Lett. 1994 Mar 14;341(1):19-22
references: 7511111
references: Biochem J. 1986 May 15;236(1):307-10
references: 3790080
references: Biochem J. 1977 Mar 1;161(3):619-25
references: 15551
references: Bioorg Med Chem. 2004 Jun 15;12(12):3239-45
references: 15158792
references: Indian J Med Res. 1980 Apr;71:632-4
references: 7390600
references: Biochim Biophys Acta. 2008 Apr;1780(4):673-9
references: 18178166
references: Folia Haematol Int Mag Klin Morphol Blutforsch. 1982;109(1):52-60
references: 6177608
references: Org Biomol Chem. 2004 Oct 21;2(20):2902-10
references: 15480453
references: Lipids. 1999 Oct;34(10):1025-9
references: 10580329
references: J Biol Chem. 1999 Oct 8;274(41):29303-10
references: 10506189
references: Biochem Pharmacol. 2004 Nov 15;68(10 ):2043-52
references: 15476675
references: Langmuir. 2009 May 19;25(10):5773-7
references: 19320475
references: J Phys Chem B. 2010 Mar 11;114(9):3348-54
references: 20148537
references: Mol Cell Biochem. 1996 Jun 21;159(2):85-93
references: 8858558
references: J Enzyme Inhib Med Chem. 2003 Dec;18(6):505-9
references: 15008515
references: Spectrochim Acta A Mol Biomol Spectrosc. 2009 Sep 15;74(1):94-9
references: 19502106
references: Biopolymers. 2009 Feb;91(2):108-19
references: 18814316
references: Life Sci. 1998;62(25):2349-58
references: 9651124
references: J Biol Chem. 2005 Jul 1;280(26):25284-90
references: 15879598
references: J Clin Invest. 1969 Mar;48(3):536-42
references: 5773090
references: Eur J Biochem. 1984 Jun 15;141(3):473-5
references: 6745254
references: J Comput Chem. 2010 Jan 30;31(2):455-61
references: 19499576
references: Planta Med. 1991 Feb;57(1):1-7
references: 2062949
references: J Alzheimers Dis. 2004 Aug;6(4):367-77; discussion 443-9
references: 15345806
references: Arch Biochem Biophys. 1964 Feb;104:297-304
references: 14163896
references: Biochim Biophys Acta. 2004 Sep 24;1674(2):205-14
references: 15374625
references: Photochem Photobiol Sci. 2012 Feb;11(2):323-32
references: 22159637
references: Eur J Biochem. 1995 Jan 15;227(1-2):563-5
references: 7851438
references: Mol Cell Biochem. 1995 Nov 8;152(1):13-21
references: 8609907
references: Indian J Exp Biol. 1979 Dec;17(12):1363-6
references: 540987
references: J Biochem. 2005 Oct;138(4):335-41
references: 16272127
references: Adv Protein Chem. 1994;45:153-203
references: 8154369
references: FEBS Lett. 1976 Jul 15;66(2):173-5
references: 955075
references: Pharmacol Rev. 1981 Mar;33(1):17-53
references: 7027277
references: J Fluoresc. 2008 Mar;18(2):519-26
references: 18097738
references: FEBS J. 2006 Dec;273(23):5320-32
references: 17069615
references: Biochem Biophys Res Commun. 2000 Oct 14;277(1):83-8
references: 11027644
references: Chem Biol Interact. 2000 Aug 15;128(1):19-38
references: 10996298
references: Chem Biol. 2003 Aug;10(8):695-704
references: 12954328
references: Photochem Photobiol. 2000 Nov;72(5):625-31
references: 11107847