Table of Contents Author Guidelines Submit a Manuscript
Journal of Spectroscopy
Volume 2015, Article ID 435674, 9 pages
http://dx.doi.org/10.1155/2015/435674
Research Article

Insight into the Interaction between the HIV-1 Integrase Inhibitor Elvitegravir and Bovine Serum Albumin: A Spectroscopic Study

Department of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, P.O. Box 2457, Riyadh 11451, Saudi Arabia

Received 2 February 2015; Revised 4 March 2015; Accepted 5 March 2015

Academic Editor: Rizwan Hasan Khan

Copyright © 2015 Ali Saber Abdelhameed. 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.

Linked References

  1. A. B. Khan, J. M. Khan, M. S. Ali, R. H. Khan, and D. Kabir-Ud, “Interaction of amphiphilic drugs with human and bovine serum albumins,” Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, vol. 97, pp. 119–124, 2012. View at Publisher · View at Google Scholar · View at Scopus
  2. X. M. He and D. C. Carter, “Atomic structure and chemistry of human serum albumin,” Nature, vol. 358, no. 6383, pp. 209–215, 1992. View at Publisher · View at Google Scholar · View at Scopus
  3. U. Kragh-Hansen, “Molecular aspects of ligand binding to serum albumin,” Pharmacological Reviews, vol. 33, no. 1, pp. 17–53, 1981. View at Google Scholar · View at Scopus
  4. A. Varshney, P. Sen, E. Ahmad, M. Rehan, N. Subbarao, and R. H. Khan, “Ligand binding strategies of human serum albumin: how can the cargo be utilized?” Chirality, vol. 22, no. 1, pp. 77–87, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. S. K. Chaturvedi, E. Ahmad, J. M. Khan, P. Alam, M. Ishtikhar, and R. H. Khan, “Elucidating the interaction of limonene with bovine serum albumin: a multi-technique approach,” Molecular BioSystems, vol. 11, no. 1, pp. 307–316, 2015. View at Publisher · View at Google Scholar
  6. P. Sen, B. Ahmad, and R. H. Khan, “Formation of a molten globule like state in bovine serum albumin at alkaline pH,” European Biophysics Journal, vol. 37, no. 8, pp. 1303–1308, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. P. Bolel, N. Mahapatra, and M. Halder, “Optical spectroscopic exploration of binding of cochineal red a with two homologous serum albumins,” Journal of Agricultural and Food Chemistry, vol. 60, no. 14, pp. 3727–3734, 2012. View at Publisher · View at Google Scholar · View at Scopus
  8. D. C. Carter and J. X. Ho, “Structure of serum albumin,” Advances in Protein Chemistry, vol. 45, pp. 153–203, 1994. View at Publisher · View at Google Scholar · View at Scopus
  9. A. A. Bhattacharya, T. Grüne, and S. Curry, “Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin,” Journal of Molecular Biology, vol. 303, no. 5, pp. 721–732, 2000. View at Publisher · View at Google Scholar · View at Scopus
  10. A. A. Spector, K. John, and J. E. Fletcher, “Binding of long-chain fatty acids to bovine serum albumin,” The Journal of Lipid Research, vol. 10, no. 1, pp. 56–67, 1969. View at Google Scholar · View at Scopus
  11. I. E. Borissevitch, T. T. Tominaga, H. Imasato, and M. Tabak, “Fluorescence and optical absorption study of interaction of two water soluble porphyrins with bovine serum albumin. The role of albumin and porphyrin aggregation,” Journal of Luminescence, vol. 69, no. 2, pp. 65–76, 1996. View at Publisher · View at Google Scholar · View at Scopus
  12. G. Blauer and T. E. King, “Interactions of bilirubin with bovine serum albumin in aqueous solution,” Journal of Biological Chemistry, vol. 245, no. 2, pp. 372–381, 1970. View at Google Scholar · View at Scopus
  13. J. Tian, J. Liu, Z. Hu, and X. Chen, “Interaction of wogonin with bovine serum albumin,” Bioorganic and Medicinal Chemistry, vol. 13, no. 12, pp. 4124–4129, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. N. Zhou, Y.-Z. Liang, and P. Wang, “18β-Glycyrrhetinic acid interaction with bovine serum albumin,” Journal of Photochemistry and Photobiology A: Chemistry, vol. 185, no. 2-3, pp. 271–276, 2007. View at Publisher · View at Google Scholar · View at Scopus
  15. Y.-Q. Wang, H.-M. Zhang, G.-C. Zhang, W.-H. Tao, Z.-H. Fei, and Z.-T. Liu, “Spectroscopic studies on the interaction between silicotungstic acid and bovine serum albumin,” Journal of Pharmaceutical and Biomedical Analysis, vol. 43, no. 5, pp. 1869–1875, 2007. View at Publisher · View at Google Scholar · View at Scopus
  16. Y. P. Wang, Y. L. Wei, and C. Dong, “Study on the interaction of 3, 3-bis(4-hydroxy-1-naphthyl)-phthalide with bovine serum albumin by fluorescence spectroscopy,” Journal of Photochemistry and Photobiology A: Chemistry, vol. 177, pp. 6–11, 2006. View at Google Scholar
  17. A. Gong, X. Zhu, Y. Hu, and S. Yu, “A fluorescence spectroscopic study of the interaction between epristeride and bovin serum albumine and its analytical application,” Talanta, vol. 73, no. 4, pp. 668–673, 2007. View at Publisher · View at Google Scholar · View at Scopus
  18. B. Zhou, Z.-D. Qi, Q. Xiao, J.-X. Dong, Y.-Z. Zhang, and Y. Liu, “Interaction of loratadine with serum albumins studied by fluorescence quenching method,” Journal of Biochemical and Biophysical Methods, vol. 70, no. 5, pp. 743–747, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. A. Sułkowska, “Interaction of drugs with bovine and human serum albumin,” Journal of Molecular Structure, vol. 614, no. 1–3, pp. 227–232, 2002. View at Publisher · View at Google Scholar · View at Scopus
  20. N. Gull, P. Sen, and R. H. Khan, “Interaction of bovine (BSA), rabbit (RSA), and porcine (PSA) serum albumins with cationic single-chain/gemini surfactants: a comparative study,” Langmuir, vol. 25, no. 19, pp. 11686–11691, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. N. Zaidi, S. Nusrat, F. K. Zaidi, and R. H. Khan, “pH-dependent differential interacting mechanisms of sodium dodecyl sulfate with bovine serum fetuin: a biophysical insight,” The Journal of Physical Chemistry B, vol. 118, no. 46, pp. 13025–13036, 2014. View at Publisher · View at Google Scholar
  22. E. J. Arts and D. J. Hazuda, “HIV-1 antiretroviral drug therapy,” Cold Spring Harbor Perspectives in Medicine, vol. 2, no. 4, Article ID a007161, 2012. View at Publisher · View at Google Scholar · View at Scopus
  23. S. L. Karmon and M. Markowitz, “Next-generation integrase inhibitors: where to after raltegravir?” Drugs, vol. 73, no. 3, pp. 213–228, 2013. View at Publisher · View at Google Scholar · View at Scopus
  24. S. Ramanathan, A. A. Mathias, P. German, and B. P. Kearney, “Clinical pharmacokinetic and pharmacodynamic profile of the HIV integrase inhibitor elvitegravir,” Clinical Pharmacokinetics, vol. 50, no. 4, pp. 229–244, 2011. View at Publisher · View at Google Scholar · View at Scopus
  25. K. Shimura, E. Kodama, Y. Sakagami et al., “Broad antiretroviral activity and resistance profile of the novel human immunodeficiency virus integrase inhibitor elvitegravir (JTK-303/GS-9137),” Journal of Virology, vol. 82, no. 2, pp. 764–774, 2008. View at Publisher · View at Google Scholar · View at Scopus
  26. J. Marinello, C. Marchand, B. T. Mott, A. Bain, C. J. Thomas, and Y. Pommier, “Comparison of raltegravir and elvitegravir on HIV-1 integrase catalytic reactions and on a series of drug-resistant integrase mutants,” Biochemistry, vol. 47, no. 36, pp. 9345–9354, 2008. View at Publisher · View at Google Scholar · View at Scopus
  27. A. R. Zolopa, D. S. Berger, H. Lampiris et al., “Activity of elvitegravir, a once-daily integrase inhibitor, against resistant HIV type 1: results of a phase 2, randomized, controlled, dose-ranging clinical trial,” The Journal of Infectious Diseases, vol. 201, no. 6, pp. 814–822, 2010. View at Publisher · View at Google Scholar · View at Scopus
  28. E. D. Deeks, “Elvitegravir: a review of its use in adults with HIV-1 infection,” Drugs, vol. 74, no. 6, pp. 687–697, 2014. View at Publisher · View at Google Scholar · View at Scopus
  29. Gilead Sciences International, Vitekta Film-Coated Tablets: EU Summary of Product Characteristics, Gilead Sciences International, 2013, http://ec.europa.eu/health/documents/community-register/2013/20131113126981/anx_126981_en.pdf.
  30. U.S. Food and Drug Administration (FDA), Approval of Vitekta, 2014, http://www.accessdata.fda.gov/drugsatfda_docs/label/2014/203093s000lbl.pdf.
  31. S. Sugio, A. Kashima, S. Mochizuki, M. Noda, and K. Kobayashi, “Crystal structure of human serum albumin at 2.5 Å resolution,” Protein Engineering, vol. 12, no. 6, pp. 439–446, 1999. View at Publisher · View at Google Scholar · View at Scopus
  32. I. Petitpas, T. Grüne, A. A. Bhattacharya, and S. Curry, “Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids,” Journal of Molecular Biology, vol. 314, no. 5, pp. 955–960, 2001. View at Publisher · View at Google Scholar · View at Scopus
  33. H.-X. Zhang, S. Gao, and X.-X. Yang, “Synthesis of an octupolar compound and its biological effects on serum albumin,” Molecular Biology Reports, vol. 36, no. 6, pp. 1405–1411, 2009. View at Publisher · View at Google Scholar · View at Scopus
  34. P. B. Kandagal, J. Seetharamappa, S. Ashoka, S. M. T. Shaikh, and D. H. Manjunatha, “Study of the interaction between doxepin hydrochloride and bovine serum albumin by spectroscopic techniques,” International Journal of Biological Macromolecules, vol. 39, no. 4-5, pp. 234–239, 2006. View at Publisher · View at Google Scholar · View at Scopus
  35. Th. Förster, “Zwischenmolekulare Energiewanderung und Fluoreszenz,” Annalen der Physik, vol. 437, no. 1-2, pp. 55–75, 1948. View at Publisher · View at Google Scholar
  36. J. R. Lakowicz, Principle of Fluorescence Spectroscopy, Plemum Press, New York, NY, USA, 2nd edition, 1999.
  37. H. Wang, J. Mao, A. Duan et al., “Fluorescence quenching of 4-tert-octylphenol by room temperature ionic liquids and its application,” Journal of Fluorescence, vol. 23, no. 2, pp. 323–331, 2013. View at Publisher · View at Google Scholar · View at Scopus
  38. G.-Z. Chen, X.-Z. Huang, and J.-G. Xu, Spectrofluorimetric Analytical Method, Science Press, Beijing, China, 2nd edition, 1990.
  39. O. Stern and M. Volmer, “The extinction period of fluorescence,” Physikalische Zeitschrift, vol. 20, pp. 183–188, 1919. View at Google Scholar
  40. H. Lineweaver and D. Burk, “The determination of enzyme dissociation constants,” Journal of the American Chemical Society, vol. 56, no. 3, pp. 658–666, 1934. View at Publisher · View at Google Scholar · View at Scopus
  41. W. R. Ware, “Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process,” The Journal of Physical Chemistry, vol. 66, no. 3, pp. 455–458, 1962. View at Publisher · View at Google Scholar · View at Scopus
  42. Y. Huang, Z. Zhang, D. Zhang, and J. Lv, “Flow-injection analysis chemiluminescence detection combined with microdialysis sampling for studying protein binding of drug,” Talanta, vol. 53, no. 4, pp. 835–841, 2001. View at Publisher · View at Google Scholar · View at Scopus
  43. J. R. Lakowicz and G. Weber, “Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules,” Biochemistry, vol. 12, no. 21, pp. 4161–4170, 1973. View at Publisher · View at Google Scholar · View at Scopus
  44. J. Liu, J.-N. Tian, J. Zhang, Z. Hu, and X. Chen, “Interaction of magnolol with bovine serum albumin: a fluorescence-quenching study,” Analytical and Bioanalytical Chemistry, vol. 376, no. 6, pp. 864–867, 2003. View at Publisher · View at Google Scholar · View at Scopus
  45. T. Forster and O. Sinanoglu, Modern Quantum Chemistry, vol. 3, Academic Press, New York, NY, USA, 1996.
  46. P. D. Ross and S. Subramanian, “Thermodynamics of protein association reactions: forces contributing to stability,” Biochemistry, vol. 20, no. 11, pp. 3096–3102, 1981. View at Publisher · View at Google Scholar · View at Scopus
  47. H.-X. Zhang, X. Huang, and M. Zhang, “Thermodynamic studies on the interaction of dioxopromethazine to β-cyclodextrin and bovine serum albumin,” Journal of Fluorescence, vol. 18, no. 3-4, pp. 753–760, 2008. View at Publisher · View at Google Scholar · View at Scopus
  48. H. D. B. Jenkins, “Gibbs-Helmholtz equation,” in Chemical Thermodynamics at a Glance, pp. 150–153, Blackwell Publishing, 2008. View at Google Scholar
  49. Z. Jannesari, H. Hadadzadeh, T. Khayamian, B. Maleki, and H. A. Rudbari, “Experimental and molecular modeling studies on the interaction of the Ru(II)-piroxicam with DNA and BSA,” European Journal of Medicinal Chemistry, vol. 69, pp. 577–590, 2013. View at Publisher · View at Google Scholar · View at Scopus
  50. B. Valeur and J. C. Brochon, New Trends in Fluorescence Spectroscopy, Springer Press, Berlin, Germany, 6th edition, 1999.
  51. Y.-J. Hu, Y. Liu, J.-B. Wang, X.-H. Xiao, and S.-S. Qu, “Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin,” Journal of Pharmaceutical and Biomedical Analysis, vol. 36, no. 4, pp. 915–919, 2004. View at Publisher · View at Google Scholar · View at Scopus
  52. W. He, Y. Li, C. Xue, Z. Hu, X. Chen, and F. Sheng, “Effect of Chinese medicine alpinetin on the structure of human serum albumin,” Bioorganic & Medicinal Chemistry, vol. 13, no. 5, pp. 1837–1845, 2005. View at Publisher · View at Google Scholar · View at Scopus
  53. F.-L. Cui, J. Fan, J.-P. Li, and Z.-D. Hu, “Interactions between 1-benzoyl-4-p-chlorophenyl thiosemicarbazide and serum albumin: investigation by fluorescence spectroscopy,” Bioorganic & Medicinal Chemistry, vol. 12, no. 1, pp. 151–157, 2004. View at Publisher · View at Google Scholar · View at Scopus
  54. H. Yan, S. Zhao, J. Yang et al., “Interaction between levamisole hydrochloride and bovine serum albumin and the influence of alcohol: spectra,” Journal of Solution Chemistry, vol. 38, no. 9, pp. 1183–1192, 2009. View at Publisher · View at Google Scholar · View at Scopus
  55. H.-X. Zhang, X. Huang, P. Mei, and S. Gao, “Interaction between glyoxal-bis-(2-hydroxyanil) and bovine serum albumin in solution,” Journal of Solution Chemistry, vol. 37, no. 5, pp. 631–640, 2008. View at Publisher · View at Google Scholar · View at Scopus
  56. A. N. Glazer and E. L. Smith, “Studies on the ultraviolet difference spectra of proteins and polypeptides,” The Journal of Biological Chemistry, vol. 236, pp. 2942–2947, 1961. View at Google Scholar · View at Scopus
  57. M. Ishtikhar, S. Khan, G. Badr, A. Osama Mohamed, and R. Hasan Khan, “Interaction of the 5-fluorouracil analog 5-fluoro-2′-deoxyuridine with ‘N’ and ‘B’ isoforms of human serum albumin: a spectroscopic and calorimetric study,” Molecular BioSystems, vol. 10, no. 11, pp. 2954–2964, 2014. View at Publisher · View at Google Scholar