Multi-spectroscopic characterization of bovine serum albumin upon interaction with atomoxetine

Journal of Pharmaceutical Analysis

Volumn 7, Issue 3, 2017, Pages 148-155

  Buddanavar, Arunkumar T ^a   Nandibewoor, Sharanappa T ^a  

^a KARNATAK UNIVERSITY   (India)

Author keywords

3D fluorescence spectra; Atomoxetine; Bovine serum albumin; Energy transfer; FT IR; Lifetime measurement

Indexed keywords

ATOMOXETINE; BOVINE SERUM ALBUMIN;

ABSORPTION SPECTROSCOPY; ARTICLE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DRUG MECHANISM; DRUG PROTEIN BINDING; ENTHALPY; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; INFRARED SPECTROSCOPY; NONHUMAN; RATE CONSTANT; THERMODYNAMICS; THREE DIMENSIONAL IMAGING; ULTRAVIOLET SPECTROSCOPY;

EID: 85015389507     PISSN: 20951779     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jpha.2016.10.001     Document Type: Article

References (46)

1. Yu, J., Li, B., Dai, P., Ge, S., Molecular simulation of the interaction between novel type rhodanine derivative probe and bovine serum albumin. Spectrochim. Acta A 74 (2009), 277–281.
2. Hu, Y.J., Liu, Y., Shen, X.S., et al. Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin. J. Mol. Struct. 738 (2005), 143–147.
3. Sandhya, B., Hegde, A.H., Kalanur, 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.
4. Zhao, H.W., Ge, M., Zhang, Z.X., et al. Spectroscopic studies on the interaction between riboflavin and albumins. Spectrochim. Acta A 65 (2006), 811–817.
5. Meti, M.D., Nandibewoor, S.T., Joshi, S.D., et al. Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin. J. Pharm. Biomed. Anal. 5 (2015), 249–255.
6. Wong, D.T., Threlkeld, P.G., Best, K.L., et al. A new inhibitor of norepinephrine uptake devoid of affinity for receptors in rat brain. J. Pharmacol. Exp. Ther. 222 (1982), 61–65.
7. 3H] atomoxetine, an enantiomerically pure ligand for norepinephrine reuptake sites. Neurosci. Lett. 157 (1993), 203–206.
8. Lee, M.J., Yang, K.C., Shyu, Y.C., et al. Attention deficit hyper activity disorder, its treatment with medication and the probability of developing a depressive disorder: a nationwide population-based study in Taiwan. J. Affect. Disord. 189 (2016), 110–117.
9. Chi, Z., Liu, R., Teng, Y., et al. Binding of oxytetracycline to bovine serum albumin: spectroscopic and molecular modeling investigations. J. Agric. Food Chem. 58 (2010), 10262–10269.
10. Gowda, J.I., Nandibewoor, S.T., Binding and conformational changes of human serum albumin upon interaction with 4-aminoantipyrine studied by spectroscopic methods and cyclic voltammetry. Spectrochim. Acta A 124 (2014), 397–403.
11. Enrico, G., Jameson, D.M., weber, G., A model of dynamic quenching of fluorescence in globular proteins. J. Biophys. 45 (1984), 789–794.
12. Lakowicz, J.R., Freshwater, G., Weber, G., Nanosecond segmental mobilities of tryptophan residues in proteins observed by lifetime resolved fluorescence anisotropies. J. Biophys. 32 (1980), 591–601.
13. Naik, K.M., Kolli, D.B., Nandibewoor, S.T., Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies. SpringerPlus 3 (2014), 360–373.
14. Zhang, Y.Z., Zhou, B., Zhang, X.P., et al. Interaction of malachite green with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods. J. Hazard. Mater. 163 (2009), 1345–1352.
15. Lakowicz, J.R., Principles of Fluorescence Spectroscopy. 3rd ed., 2006, Plenum Press, New York, 280.
16. Ware, W.R., Oxygen quenching of fluorescence in solution an experimental study of the diffusion process. J. Phys. Chem. 66 (1962), 455–458.
17. Punith, R., Seetharamappa, J., Spectral characterization of the binding and conformational changes of serum albumins upon interaction with an anticancer drug anastrozole. Spectrochim. Acta A. 92 (2012), 37–41.
18. Zhao, X.C., Liu, R.T., Chi, Z.X., et al. New insights into the behavior of bovine serum albumin adsorbed onto carbon nanotubes comprehensive spectroscopic studies. J. Phys. Chem. B 114 (2010), 5625–5631.
19. Lakowicz, J.R., Weber, G., Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. Biochemistry 12 (1973), 4161–4170.
20. Maciejewski, A., Demmer, D.R., James, D.R., et al. Relaxation of the second excited singlet states of aromatic thiones: the role of specific solute-solvent interactions. J. Am. Chem. Soc. 107 (1985), 2831–2837.
21. Hu, Y.J., Liu, Y., Wang, J.B., et al. Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. J. Pharm. Biomed. Anal. 36 (2004), 915–919.
22. Li, Y., He, W., Liu, J., et al. Binding of the bioactive component jatrorrhizine to human serum albumin. Biochim. Biophys. Acta 1722 (2005), 15–21.
23. Ross, P.D., Subramanian, S., Thermodynamics of protein association reactions forces contributing to stability. Biochemistry 20 (1981), 3096–3102.
24. Lu, J.Q., Jin, F., Sun, T.Q., et al. Multi-spectroscopic study on interaction of bovine serum albumin with lomefloxacin–copper(II) complex. Int. J. Biol. Macromolec. 40 (2007), 299–306.
25. Guo, X.J., Zhang, L., Sun, X.D., Spectroscopic studies on the interaction between sodium ozagrel and bovine serum albumin. J. Mol. Struct. 928 (2009), 114–120.
26. Zhang, Y.Z., Zhang, X.P., Hou, H.N., Study on the interaction between Cu (phen)23þ and bovine serum albumin by spectroscopic methods. Biol. Trace Elem. Res. 121 (2008), 276–287.
27. P. Held, Quantitation of Peptides and Amino Acids with a Synergy™HT using UV Fluorescence BioTek Instruments, Inc., Highland Park, Winooski, Vermont 05404-0998 USA, 〈 www.biotek.com〉.
28. Schmid, F.X., Biological Macromolecules, UV-visible Spectrophotometry, Encyclopedia of Life Sciences. 2001, Macmillan Publishers Ltd, Nature Publishing Group, University of Bayreuth, Germany.
29. Naik, D.B., Moorty, P.N., Priyadarsini, K.I., Nonradiative energy transfer from 7-amino coumarin dyes to thiazine dyes in methanolic solutions. Chem. Phys. Lett. 168 (1990), 533–538.
30. Förster, T., 10th Spiers memorial lecture. Transfer mechanisms of electronic excitation. Discuss. Faraday Soc. 27 (1959), 7–17.
31. Cyril, L., Earl, J.K., Sperry, W.M., Biochemist's Hand Book. 1961, E&FN Epon Led. Press, London.
32. Hu, Y.J., Liu, Y., Zhang, L.X., Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method. J. Mol. Struct. 750 (2005), 174–178.
33. Lin, H., Lan, J., Guan, M., et al. Spectroscopic investigation of interaction between mangiferin and bovine serum albumin. Spectrochim. Acta A 73 (2009), 936–941.
34. Jiang, X.Y., Li, W.X., Cao, H., Study of the interaction between trans-resveratrol and BSA by the multi-spectroscopic method. J. Solut. Chem. 37 (2008), 1609–1623.
35. Brustein, E.A., Vedenkina, N.S., Irkova, M.N., fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 18 (1973), 263–279.
36. Lu, Z.X., Cui, T., Shi, Q.L., Applications of Circular Dichroism and Optical Rotatory Dispersion in Molecular Biology. 1st ed., 1987, Science Press, Marrickville, 79–82.
37. Guo, X.J., Hao, A.J., Han, X.W., The investigation of the interaction between ribavirin and bovine serum albumin by spectroscopic methods. Mol. Biol. Rep. 38 (2011), 4185–4192.
38. Shaikh, S.M.T., Seetharamappa, J., Kandagal, P.B., et al. Spectroscopic investigations on the mechanism of interaction of bioactive dye with bovine serum albumin. Dyes Pigments 74 (2007), 665–671.
39. Zhang, H.X., Mei, P., In vitro binding of furadan to bovine serum albumin. J. Sol. Chem. 38 (2009), 351–361.
40. Tian, J.N., Liu, J.Q., Hu, Z.D., et al. Interaction of wogonin with bovine serum albumin. Bioorg. Med. Chem. 13 (2005), 4124–4129.
41. Liu, Y., Yang, Z., Du, J., et al. Interaction of curcumin with intravenous immunoglobulin: a fluorescence quenching and Fourier transformation infrared spectroscopy study. Immunobiology 213 (2008), 651–661.
42. Harding, S.E., Chardhry, B.Z., Protein Ligand Interactions: Structure and Spectroscopy. 2001, Oxford University Press, Oxford.
43. Brauner, J.W., Flach, C.R., Mendelsohn, R., A quantitative reconstruction of the amide I contour in the IR spectra of globular proteins: from structure to spectrum. J. Am. Chem. Soc. 127 (2005), 100–109.
44. Zhang, Y., Yang, Y., Guo, T., Genipin-crosslinked hydrophobical chitosan microspheres and their interactions with bovine serum albumin. Carbohydr. Polym. 83 (2011), 2016–2021.
45. 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.
46. Sjoholm, I., Ekman, B., Kober, A., et al. Binding of drugs to human serum albumin: XI. The specificity of three binding sites as studied with albumin immobilized in microparticles. Mol. Pharmacol. 16 (1979), 767–777.