Effects of urea, metal ions and surfactants on the binding of baicalein with bovine serum albumin

Journal of Pharmaceutical Analysis

Volumn 6, Issue 4, 2016, Pages 256-267

  Roy, Atanu Singha ^a   Dinda, Amit Kumar ^a   Pandey, Nitin Kumar ^a   Dasgupta, Swagata ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY   (India)

Author keywords

Baicalein; Binding constant; Bovine serum albumin (BSA); Fluorescence spectroscopy; Molecular docking

Indexed keywords

BAICALEIN; BOVINE SERUM ALBUMIN; COBALT; DODECYL SULFATE SODIUM; MAGNESIUM ION; MANGANESE; METAL ION; NICKEL; SILVER; SURFACTANT; UREA; ZINC ION;

ARTICLE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DRUG PROTEIN BINDING; ENERGY TRANSFER; ENTHALPY; FLUORESCENCE; HYDROPHOBICITY; INFRARED SPECTROSCOPY; LIGAND BINDING; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR DOCKING; PROTEIN REFOLDING; PROTEIN UNFOLDING; STATIC ELECTRICITY;

EID: 84991209253     PISSN: 20951779     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jpha.2016.04.001     Document Type: Article

References (69)

1. [1] Kragh-Hansen, U., Molecular aspects of ligand binding serum albumin. Pharmacol. Rev. 33 (1981), 17–53.
2. [2] Zunszain, P.A., Ghuman, J., Komatsu, T., et al. Crystal structural analysis of human serum albumin complexed with hemin and fatty acids. BMC Struct. Biol. 3 (2003), 6–14.
3. [3] Sugio, S., Kashima, A., Mochizuki, S., et al. Crystal structure of human serum albumin at 2.5 Å resolution. Protein Eng. 12 (1999), 439–446.
4. [4] Carter, D.C., Chang, B., Ho, J.X., et al. Preliminary crystallographic studies of four crystal forms of serum albumin. Eur. J. Biochem. 226 (1994), 1049–1052.
5. [5] He, H.M., Carter, D.C., Atomic structure and chemistry of human serum albumin. Nature 358 (1992), 209–215.
6. [6] Petitpas, I., Bhattacharya, A.A., Twine, S., et al. Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I. J. Biol. Chem. 276 (2001), 22804–22809.
7. [7] Ghuman, J., Zunszain, P.A., Petitpas, I., et al. Crystal structure analysis of warfarin binding to human serum albumin. Anatomy of drug site I. J. Mol. Biol. 353 (2005), 38–52.
8. [8] Peterman, B.F., Laidler, K.J., Study of reactivity of tryptophan residues in serum albumins and lysozyme by N-bromosuccinamide fluorescence quenching. Arch. Biochem. Biophys. 199 (1980), 158–164.
9. [9] Matei, I., Ionescu, S., Hillebrand, M., Interaction of fisetin with human serum albumin by fluorescence, circular dichroism spectroscopy and DFT calculations: binding parameters and conformational changes. J. Lumin. 131 (2011), 1629–1635.
10. [10] Singha Roy, A., Tripathy, D.R., Chatterjee, A., et al. A spectroscopic study of the interaction of the antioxidant naringin with bovine serum albumin. J. Biophys. Chem. 1 (2010), 141–152.
11. [11] Matei, I., Hillebrand, M., Interaction of kaempferol with human serum albumin: a fluorescence and circular dichroism study. J. Pharm. Biomed. Anal. 51 (2010), 768–773.
12. [12] Wang, L., Ling, Y., Chen, Y., et al. Flavonoid baicalein suppresses adhesion, migration and invasion of MDA-MB-231 human breast cancer cells. Cancer Lett. 297 (2010), 42–48.
13. [13] Deschamps, J.D., Kenyon, V.A., Holman, T.R., Baicalein is a potent in vitro inhibitor against both reticulocyte 15-human and platelet 12-human lipoxygenases. Bioorg. Med. Chem. 14 (2006), 4295–4301.
14. [14] Pu, P., Wang, X.A., Salim, M., et al. Baicalein, a natural product, selectively activating AMPKα(2) and ameliorates metabolic disorder in diet-induced mice. Mol. Cell. Endocrinol. 262 (2012), 128–138.
15. [15] Liang, R.R., Zhang, S., Qi, J.A., et al. Preferential inhibition of hepatocellular carcinoma by the flavonoid Baicalein through blocking MEK-ERK signaling. Int. J. Oncol. 41 (2012), 969–978.
16. [16] Zhang, Z., Cui, W., Li, G., et al. Baicalein protects against 6-OHDA-induced neurotoxicity through activation of Keap1/Nrf2/HO-1 and involving PKCα and PI3K/AKT signaling pathways. J. Agric. Food Chem. 60 (2012), 8171–8182.
17. [17] Oh, K.S., Oh, B.K., Park, C.H., et al. Baicalein potently inhibits Rho kinase activity and suppresses actin stress fiber formation in angiotensin II-stimulated H9c2 cells. Biol. Pharm. Bull. 35 (2012), 1281–1286.
18. [18] Xiao, J., Kai, G., A review of dietary polyphenol-plasma protein interactions: characterization, influence on the bioactivity, and structure-affinity relationship. Crit. Rev. Food Sci. Nutr. 52 (2012), 85–101.
19. [19] Xiao, J., Polyphenol-plasma proteins interaction: its nature, analytical techniques, and influence on bioactivities of polyphenols. Curr. Drug Metab. 14 (2013), 367–368.
20. 3+by spectroscopic approaches. Eur. J. Med. Chem. 46 (2011), 588–599.
21. [21] Pace, C.N., Vajdos, F., Fee, L., et al. How to measure and predict the molar absorption coefficient of a protein?. Protein Sci. 4 (1995), 2411–2423.
22. [22] Perry, J.L., Goldsmith, M.R., Williams, T.R., et al. Binding of warfarin influences the acid-base equilibrium of H242 in sudlow site I of human serum albumin. Photochem. Photobiol. 82 (2006), 1365–1369.
23. [23] Tang, J.H., Luan, F., Chen, X.G., Binding analysis of glycyrrhetinic acid to human serum albumin: fluorescence spectroscopy, FT-IR, and molecular modeling. Bioorg. Med. Chem. 14 (2006), 3210–3217.
24. [24] Whitmore, L., Wallace, B.A., DICHROWEB: an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004), W668–W673.
25. [25] Byler, D.M., Susi, H., Examination of the secondary structure of proteins by deconvolved FT-IR spectra. Biopolymers 25 (1986), 469–487.
26. [26] Bujacz, A., Structures of bovine, equine and leporine serum albumin. Acta Crystallogr. D 68 (2012), 1278–1289.
27. [27] Berman, H.M., Westbrook, J., Feng, Z., et al. The protein data bank. Nucleic Acids Res. 28 (2000), 235–242.
28. [28] DeLano, W.L., The PyMoL molecular graphics system. 2004, DeLano Scientific, San Carlos, CA, USA 〈http://www.pymol.sourceforge.net〉.
29. [29] S.J. Hubbard, J.M. Thornton, NACCESS. Computer program, Department of Biochemistry and Molecular Biology, University College of London, 1993.
30. [30] Sahoo, B.K., Ghosh, K.S., Dasgupta, S., Investigating the binding of curcumin derivatives to bovine serum albumin. Biophys. Chem. 132 (2008), 81–88.
31. [31] Mabry, T.J., Markham, K.R., Thomas, M.B., The Systematic Identification of Flavonoids, 1970, Springer-Verlag, New York, 41–164.
32. [32] Zsila, F., Bikadi, Z., Simonyi, M., Probing the binding of the flavonoid, quercetin to human serum albumin by circular dichroism, electronic absorption spectroscopy and molecular modeling studies. Biochem. Pharmacol. 65 (2003), 447–456.
33. [33] Benesi, H.A., Hildebrand, J.H., A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons. J. Am. Chem. Soc. 71 (1949), 2703–2707.
34. [34] Lakowicz, J.R., Principles of Fluorescence Spectroscopy, 2006, Springer, New York, 278–284.
35. [35] Bi, S., Yan, L., Sun, Y., et al. Investigation of ketoprofen binding to human serum albumin by spectral methods. Spectrochim. Acta A 78 (2011), 410–414.
36. [36] Chi, Z., Liu, R., Phenotypic characterization of the binding of tetracycline to human serum albumin. Biomacromolecules 12 (2011), 203–209.
37. [37] Su, T.J., Lu, J.R., Thomas, R.K., et al. The conformational structure of bovine serum albumin layers adsorbed at the silica-water interface. J. Phys. Chem. B 102 (1998), 8100–8108.
38. [38] Michnik, A., Michalik, K., Drzazga, Z., Stability of bovine serum albumin at different pH. J. Therm. Anal. Calorim. 80 (2005), 399–406.
39. [39] Yoshizuka, K., Ohta, H., Inoue, K., et al. Selective separation of flavonoids with a polyvinyl alcohol membrane. J. Membr. Sci. 118 (1996), 41–48.
40. [40] Xie, M.X., Xu, X.Y., Wang, Y.D., Interaction between hesperetin and human serum albumin revealed by spectroscopic methods. Biochim. Biophys. Acta 1724 (2005), 215–224.
41. [41] Li, D., Zhang, T., Xu, B.C., et al. Effect of pH on the interaction of baicalein with lysozyme by spectroscopic approaches. J. Photochem. Photobiol. B: Biol. 104 (2011), 414–424.
42. [42] Marković, Z.S., Marković, J.M.D., Milenković, D., et al. Mechanistic study of the structure–activity relationship for the free radical scavenging activity of baicalein. J. Mol. Model. 17 (2011), 2575–2584.
43. [43] Xiao, J.B., Shi, J., Cao, H., et al. Analysis of binding interaction between puerarin and bovine serum albumin by multi-spectroscopic method. J. Pharm. Biomed. Anal. 45 (2007), 609–615.
44. [44] Li, D., Wang, Y., Chen, J., et al. Characterization of the interaction between farrerol and bovine serum albumin by fluorescence and circular dichroism. Spectrochim. Acta A 79 (2011), 680–686.
45. [45] Singha Roy, A., Tripathy, D.R., Chatterjee, A., et al. The influence of common metal ions on the interactions of the isoflavone genistein with bovine serum albumin. Spectrochim. Acta A 102 (2013), 393–402.
46. [46] Ross, P.D., Subramanian, S., Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20 (1981), 3096–3102.
47. [47] Nozaki, Y., Reynolds, J.A., Tanford, C., Interaction of a cationic detergent with bovine serum-albumin and other proteins. J. Biol. Chem. 249 (1974), 4452–4459.
48. [48] Nielsen, A.D., Borch, K., Westh, P., Thermochemistry of the specific binding of C12 surfactants to bovine serum albumin. Biochim. Biophys. Acta 1479 (2000), 321–331.
49. [49] Deep, S., Ahluwalia, J.C., Interaction of bovine serum albumin with anionic surfactants. Phys. Chem. Chem. Phys. 3 (2001), 4583–4591.
50. [50] Yaseen, Z.G., On the interactions of bovine serum albumin with some surfactants: New insights from conductivity studies. J. Chem. Pharm. Res. 4 (2012), 3361–3367.
51. [51] Singh, S.K., Kishore, N., Thermodynamic insights into the binding of triton X-100 to globular proteins: a calorimetric and spectroscopic investigation. J. Phys. Chem. B 110 (2006), 9728–9737.
52. [52] Sudlow, G., Birkett, D.J., Wade, D.N., The characterization of two specific drug binding sites on human serum albumin. Mol. Pharmacol. 11 (1975), 824–832.
53. [53] Sudlow, G., Birkett, D.J., Wade, D.N., Further characterization of specific drug binding sites on human serum albumin. Mol. Pharmacol. 12 (1976), 1052–1061.
54. [54] Singha Roy, A., Ghosh, K.S., Dasgupta, S., An investigation into the altered binding mode of green tea polyphenols with human serum albumin on complexation with copper. J. Biomol. Struct. Dyn. 31 (2013), 1191–1206.
55. [55] Singha Roy, A., Pandey, N.K., Dasgupta, S., Preferential binding of fisetin to the native state of bovine serum albumin: spectroscopic and docking studies. Mol. Biol. Rep. 40 (2013), 3239–3253.
56. [56] Gokara, M., Sudhamalla, B., Amroou, D.G., et al. Molecular interaction studies of trimethoxy flavone with human serum albumin. Plos One, 5, 2010, e8834.
57. [57] Neelam, S., Gokara, M., Sudhamalla, B., et al. Interaction studies of coumaroyltyramine with human serum albumin and its biological importance. J. Phys. Chem. B 114 (2010), 3005–3012.
58. [58] Elliott, A., Ambrose, E.J., Structure of synthetic polypeptides. Nature 165 (1950), 921–922.
59. [59] Krimm, S., Bandekar, J., Vibrational spectroscopy and conformation of peptides, polypeptides and proteins. Adv. Protein Chem. 38 (1986), 181–364.
60. [60] Bourassa, P., Kanakis, C.D., Tarantilis, P., et al. Resveratrol, genistein, and curcumin bind bovine serum albumin. J. Phys. Chem. B 114 (2010), 3348–3354.
61. [61] Sandhya, B., Hedge, A.H., Klankur, S.S., et al. Interaction of triprolidine hydrochloride with serum albumins: Thermodynamic and binding characteristics, and influence of site probes. J. Pharm. Biomed. Anal. 54 (2011), 1180–1186.
62. [62] Paul, B.K., Samanta, A., Guchhait, N., Exploring hydrophobic subdomain IIA of the protein bovine serum albumin in the native, intermediate, unfolded, and refolded states by a small fluorescence molecular reporter. J. Phys. Chem. B 114 (2010), 6183–6196.
63. [63] Patra, D., Barakat, C., Tafech, R.M., Study on effect of lipophilic curcumin on sub-domain IIA site of human serum albumin during unfolded and refolded states: a synchronous fluorescence spectroscopic study. Colloids Surf. B 94 (2012), 351–361.
64. [64] Barakat, C., Patra, D., Combining time-resolved fluorescence with synchronous fluorescence spectroscopy to study bovine serum albumin-curcumin complex during unfolding and refolding processes. Luminescence 28 (2012), 149–155.
65. [65] Ojha, B., Das, G., The interaction of 5-(alkoxy)naphthalen-1-amine with bovine serum albumin its effect on the conformation of protein. J. Phys. Chem. B 114 (2010), 3979–3986.
66. [66] Abou-Zied, O.K., Al-Shihi, O.I.K., Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded and refolded states using small molecular probes. J. Am. Chem. Soc. 130 (2008), 10793–10801.
67. [67] Roy, D., Dutta, S., Maity, S.S., et al. Spectroscopic and docking studies of the binding of two stereoisomeric antioxidant catechins to serum albumins. J. Lumin. 132 (2012), 1364–1375.
68. [68] Singha Roy, A., Tripathy, D.R., Dasgupta, S., An alternate mode of binding of the polyphenol quercetin with serum albumins when complexed with Cu(II). J. Lumin. 132 (2012), 2943–2951.
69. [69] Han, L.Y., Lin, H.H., Li, Z.R., et al. PEARLS: program for energetic analysis of receptor-ligand system. J. Chem. Inf. Model. 46 (2006), 445–450.