Table of Contents
International Journal of Spectroscopy
Volume 2016, Article ID 1378680, 12 pages
http://dx.doi.org/10.1155/2016/1378680
Research Article

Interaction of Small Zinc Complexes with Globular Proteins and Free Tryptophan

1Department of Chemistry, Susquehanna University, 514 University Avenue, Selinsgrove, PA 17870, USA
2Math & Natural Sciences Department, Centenary College, 400 Jefferson Street, Hackettstown, NJ 07840, USA

Received 19 October 2015; Revised 21 December 2015; Accepted 29 December 2015

Academic Editor: Shigehiko Takegami

Copyright © 2016 Joann M. Butkus et al. 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. D. W. Christianson and C. A. Fierke, “Carbonic anhydrase: evolution of the zinc binding site by nature and by design,” Accounts of Chemical Research, vol. 29, no. 7, pp. 331–339, 1996. View at Publisher · View at Google Scholar · View at Scopus
  2. G. B. Rao, “Recent developments in the design of specific Matrix metalloproteinase inhibitors aided by structural and computational studies,” Current Pharmaceutical Design, vol. 11, no. 3, pp. 295–322, 2005. View at Publisher · View at Google Scholar
  3. C. I. Branden, H. Eklund, B. Nordstrom et al., “Structure of liver alcohol dehydrogenase at 2.9-angstrom resolution,” Proceedings of the National Academy of Sciences of the United States of America, vol. 70, no. 8, pp. 2439–2442, 1973. View at Publisher · View at Google Scholar
  4. F. A. Quiocho and W. N. Lipscomb, “Carboxypeptidase a: a protein and an enzyme,” Advances in Protein Chemistry, vol. 25, pp. 1–78, 1971. View at Publisher · View at Google Scholar · View at Scopus
  5. B. W. Matthews, “Structural basis of the action of thermolysin and related zinc peptidases,” Accounts of Chemical Research, vol. 21, no. 9, pp. 333–340, 1988. View at Publisher · View at Google Scholar · View at Scopus
  6. C. M. Overall and C. López-Otín, “Strategies for MMP inhibition in cancer: innovations for the post-trial era,” Nature Reviews Cancer, vol. 2, no. 9, pp. 657–672, 2002. View at Publisher · View at Google Scholar · View at Scopus
  7. M. M. Yamashita, L. Wesson, G. Eisenman, and D. Eisenberg, “Where metal ions bind in proteins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 15, pp. 5648–5652, 1990. View at Publisher · View at Google Scholar · View at Scopus
  8. T. Dudev and C. Lim, “Principles governing Mg, Ca, and Zn binding and selectivity in proteins,” Chemical Reviews, vol. 103, no. 3, pp. 773–788, 2003. View at Publisher · View at Google Scholar · View at Scopus
  9. I. L. Alberts, K. Nadassy, and S. J. Wodak, “Analysis of zinc binding sites in protein crystal structures,” Protein Science, vol. 7, no. 8, pp. 1700–1716, 1998. View at Publisher · View at Google Scholar · View at Scopus
  10. H. Vorum, K. Fisker, and B. Honoré, “Palmitate and stearate binding to human serum albumin: determination of relative binding constants,” Journal of Peptide Research, vol. 49, no. 4, pp. 347–354, 1997. View at Google Scholar · View at Scopus
  11. G. Zolese, G. Falcioni, E. Bertoli et al., “Steady-state and time resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines,” Proteins: Structure, Function and Genetics, vol. 40, no. 1, pp. 39–48, 2000. View at Google Scholar · View at Scopus
  12. J.-P. Laussac and B. Sarkar, “Characterization of the copper(II)- and nickel(II)-transport site of human serum albumin. Studies of copper(II) and nickel(II) binding to peptide 1–24 of human serum albumin by 13C and 1H NMR spectroscopy,” Biochemistry, vol. 23, no. 12, pp. 2832–2838, 1984. View at Publisher · View at Google Scholar · View at Scopus
  13. W. Bal, J. Christodoulou, P. J. Sadler, and A. Tucker, “Multi-metal binding site of serum albumin,” Journal of Inorganic Biochemistry, vol. 70, no. 1, pp. 33–39, 1998. View at Publisher · View at Google Scholar · View at Scopus
  14. P. Gosling, “Albumin and the critically ill,” Care Critically, vol. 11, pp. 57–61, 1995. View at Google Scholar
  15. T. Peters Jr., “Serum albumin,” Advances in Protein Chemistry, vol. 37, pp. 161–245, 1985. View at Publisher · View at Google Scholar · View at Scopus
  16. T. Peters, All about Albumin: Biochemistry, Genetics and Medical Applications, Academic Press, San Diego, Calif, USA, 1995.
  17. J. Tian, J. Liu, X. Tian, Z. Hu, and X. Chen, “Study of the interaction of kaempferol with bovine serum albumin,” Journal of Molecular Structure, vol. 691, no. 1–3, pp. 197–202, 2004. View at Publisher · View at Google Scholar · View at Scopus
  18. A. Sułkowska, J. Równicka, B. Bojko, and W. Sułkowski, “Interaction of anticancer drugs with human and bovine serum albumin,” Journal of Molecular Structure, vol. 651–653, pp. 133–140, 2003. View at Publisher · View at Google Scholar · View at Scopus
  19. Y. Li, W. He, J. Liu, F. Sheng, Z. Hu, and X. Chen, “Binding of the bioactive component Jatrorrhizine to human serum albumin,” Biochimica et Biophysica Acta—General Subjects, vol. 1722, no. 1, pp. 15–21, 2005. View at Publisher · View at Google Scholar · View at Scopus
  20. 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
  21. I. D. Kuntz, “Structure-based strategies for drug design and discovery,” Science, vol. 257, no. 5073, pp. 1078–1082, 1992. View at Publisher · View at Google Scholar · View at Scopus
  22. N. Latha and B. Jayaram, “A binding affinity based computational pathway for active-site directed lead molecule design: Some promises and perspectives,” Drug Design Reviews Online, vol. 2, no. 2, pp. 145–165, 2005. View at Publisher · View at Google Scholar · View at Scopus
  23. M. R. Eftink and C. A. Ghiron, “Dynamics of a protein matrix revealed by fluorescence quenching,” Proceedings of the National Academy of Sciences of the United States of America, vol. 72, no. 9, pp. 3290–3294, 1975. View at Publisher · View at Google Scholar · View at Scopus
  24. M. R. Eftink and C. A. Ghiron, “Fluorescence quenching studies with proteins,” Analytical Biochemistry, vol. 114, no. 2, pp. 199–227, 1981. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Eftink, “Quenching-resolved emission anisotropy studies with single and multitryptophan-containing proteins,” Biophysical Journal, vol. 43, no. 3, pp. 323–334, 1983. View at Publisher · View at Google Scholar · View at Scopus
  26. T. Imoto, L. S. Forster, J. A. Rupley, and F. Tanaka, “Fluorescence of lysozyme: emissions from tryptophan residues 62 and 108 and energy migration,” Proceedings of the National Academy of Sciences of the United States of America, vol. 69, no. 5, pp. 1151–1155, 1972. View at Publisher · View at Google Scholar · View at Scopus
  27. T. Imoto, L. N. Johnson, A. T. C. North, D. C. Phillips, and J. A. Rupley, Lysozyme in Enzymes, Academic Press, New York, NY, USA, 1972.
  28. M. J. Kronman and L. G. Holmes, “The fluorescence of native, denatured and reduced-denatured proteins,” Photochemistry and Photobiology, vol. 14, no. 2, pp. 113–134, 1971. View at Publisher · View at Google Scholar
  29. S. S. Lehrer, “Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion,” Biochemistry, vol. 10, no. 17, pp. 3254–3263, 1971. View at Publisher · View at Google Scholar · View at Scopus
  30. C. Formoso and L. S. Forster, “Tryptophan fluorescence lifetimes in lysozyme,” The Journal of Biological Chemistry, vol. 250, no. 10, pp. 3738–3745, 1975. View at Google Scholar · View at Scopus
  31. A. J. Gordon and R. A. Ford, The Chemist's Companion, John Wiley & Sons, New York, NY, USA, 1972.
  32. J. A. Riddick, W. B. Bunger, and T. K. Sakano, Organic Solvents, John Wiley & Sons, New York, NY, USA, 1986.
  33. C. M. Schneck, A. J. Poncheri, J. T. Jennings, D. L. Snyder, J. L. Worlinsky, and S. Basu, “Competition between solvent quenching and indole quenching of 9-fluorenone: a spectroscopic and computational study,” Spectrochimica Acta A: Molecular and Biomolecular Spectroscopy, vol. 75, no. 2, pp. 624–628, 2010. View at Publisher · View at Google Scholar · View at Scopus
  34. J. R. Lakowicz, Principles of Fluorescence Spectroscopy, Springer Science & Business Media, New York, NY, USA, 2004.
  35. J. S. Johansson, “Binding of the volatile anesthetic chloroform to albumin demonstrated using tryptophan fluorescence quenching,” The Journal of Biological Chemistry, vol. 272, no. 29, pp. 17961–17965, 1997. View at Publisher · View at Google Scholar · View at Scopus
  36. R. Swaminathan, G. Krishnamoorthy, and N. Periasamy, “Similarity of fluorescence lifetime distributions for single tryptophan proteins in the random coil state,” Biophysical Journal, vol. 67, no. 5, pp. 2013–2023, 1994. View at Publisher · View at Google Scholar · View at Scopus
  37. H. M. Rawel, S. K. Frey, K. Meidtner, J. Kroll, and F. J. Schweigert, “Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence,” Molecular Nutrition and Food Research, vol. 50, no. 8, pp. 705–713, 2006. View at Publisher · View at Google Scholar · View at Scopus
  38. D. Wu, Q. Wei, Y. Li, B. Du, and G. Xu, “Quenching of the intrinsic fluorescence of bovine serum albumin by phenylfluorone-Mo(VI) complex as a probe,” International Journal of Biological Macromolecules, vol. 37, no. 1-2, pp. 69–72, 2005. View at Publisher · View at Google Scholar · View at Scopus
  39. J. B. Xiao, J. W. Chen, H. Cao et al., “Study of the interaction between baicalin and bovine serum albumin by multi-spectroscopic method,” Journal of Photochemistry and Photobiology A: Chemistry, vol. 191, no. 2-3, pp. 222–227, 2007. View at Publisher · View at Google Scholar · View at Scopus
  40. D. T. Sawyer and P. J. Paulsen, “Properties and infrared spectra of ethylenediaminetetraacetic acid complexes. II. Chelates of divalent ions,” Journal of the American Chemical Society, vol. 81, no. 4, pp. 816–820, 1959. View at Publisher · View at Google Scholar · View at Scopus
  41. H. F. Crouse, J. Potoma, F. Nejrabi, D. L. Snyder, B. S. Chohan, and S. Basu, “Quenching of tryptophan fluorescence in various proteins by a series of small nickel complexes,” Dalton Transactions, vol. 41, no. 9, pp. 2720–2731, 2012. View at Publisher · View at Google Scholar · View at Scopus
  42. D. C. Weatherburn, E. J. Billo, J. P. Jones, and D. W. Margerum, “Effect of ring size on the stability of polyamine complexes containing linked consecutive rings,” Inorganic Chemistry, vol. 9, no. 6, pp. 1557–1559, 1970. View at Publisher · View at Google Scholar · View at Scopus
  43. T. G. Campbell and F. L. Urbach, “Synthesis and characterization of nickel(II) complexes of neutral, tetradentate Schiff base ligands derived from 1,3-diamines,” Inorganic Chemistry, vol. 12, no. 8, pp. 1836–1840, 1973. View at Publisher · View at Google Scholar · View at Scopus
  44. G. S. Smith and J. L. Hoard, “The structure of dihydrogen ethylenediaminetetraacetatoaquonickel(II),” Journal of the American Chemical Society, vol. 81, no. 3, pp. 556–561, 1959. View at Publisher · View at Google Scholar · View at Scopus
  45. P. Pfeiffer, E. Breith, E. Lübbe, and T. Tsumaki, “Tricyclische orthokondensierte Nebenvalenzringe,” Justus Liebig's Annalen der Chemie, vol. 503, no. 1, pp. 84–130, 1933. View at Publisher · View at Google Scholar
  46. F. Basolo and W. R. Matoush, “Changes in configuration of some nickel(II) complexes,” Journal of the American Chemical Society, vol. 75, no. 22, pp. 5663–5666, 1953. View at Publisher · View at Google Scholar · View at Scopus
  47. G. N. Tyson Jr. and S. C. Adams, “The configuration of some cupric, nickelous and cobaltous complexes by means of magnetic measurements,” Journal of the American Chemical Society, vol. 62, no. 5, pp. 1228–1229, 1940. View at Publisher · View at Google Scholar · View at Scopus
  48. A. Simion, C. Simion, T. Kanda et al., “Synthesis of imines, diimines and macrocyclic diimines as possible ligands, in aqueous solution,” Journal of the Chemical Society. Perkin Transactions 1, pp. 2071–2078, 2001. View at Google Scholar · View at Scopus
  49. A. Hantzsch and O. Schwab, “Zur kenntniss der condensationsproducte aus aldehyden und aminen,” Berichte der Deutschen Chemischen Gesellschaft, vol. 34, no. 1, pp. 822–839, 1901. View at Publisher · View at Google Scholar
  50. R. C. Aggarwal, N. K. Singh, and R. P. Singh, “Synthesis and structural studies of some first row transition metal complexes of salicylaldehyde hydrazone,” Inorganica Chimica Acta, vol. 32, no. C, pp. L87–L90, 1979. View at Publisher · View at Google Scholar · View at Scopus
  51. E. C. Okafor, “On the condensation of salicylaldehyde with hydrazine,” Talanta, vol. 25, no. 4, pp. 241–242, 1978. View at Publisher · View at Google Scholar · View at Scopus
  52. M. P. Jain and S. Kumar, “Condensation of some substituted salicylaldehydes with hydrazine,” Talanta, vol. 26, no. 9, pp. 909–910, 1979. View at Publisher · View at Google Scholar · View at Scopus
  53. R.-B. Xu, X.-Y. Xu, P.-F. Shi et al., “Synthesis and crystal structure of a new complex [bis(dien)zinc(II)] zinc(II) tetrachloride (dien = diethylenetriamine),” Chinese Journal Structural Chemistry, vol. 26, no. 12, pp. 1441–1444, 2007. View at Google Scholar
  54. L. Cheng, Y.-Y. Sun, Y.-W. Zhang, and G. Xu, “Tris(ethyl-enediamine)zinc(II) dichloride monohydrate,” Acta Crystallographica Section E: Structure Reports Online, vol. 64, no. 10, Article ID m1246, 2008. View at Publisher · View at Google Scholar · View at Scopus
  55. C. Muralikrishna, C. Mahadevan, S. Sastry, M. Seshasayee, and S. Subramanian, “Structure of tris(ethylenediamine)zinc(II) chloride dihydrate, [Zn(C2H8N2)3]Cl2.2H2O,” Acta Crystallographica, vol. 39, pp. 1630–1632, 1983. View at Publisher · View at Google Scholar
  56. S. Zhicheng, Y. Zhiming, A. Lata, and H. Yuhua, “Serum angiotensin converting enzyme, ceruloplasmin, and lactic dehydrogenase in anthracosilicosis and anthracosilicotuberculosis,” British Journal of Industrial Medicine, vol. 43, no. 9, pp. 642–643, 1986. View at Google Scholar · View at Scopus
  57. A. B. P. Lever, Inorganic Electronic Spectroscopy, Elsevier Science, Amsterdam, The Netherlands, 2nd edition, 1984.
  58. I. E. Borissevitch, “More about the inner filter effect: corrections of Stern-Volmer fluorescence quenching constants are necessary at very low optical absorption of the quencher,” Journal of Luminescence, vol. 81, no. 3, pp. 219–224, 1999. View at Publisher · View at Google Scholar · View at Scopus
  59. O. Dömötör, T. Tuccinardi, D. Karcz, M. Walsh, B. S. Creaven, and É. A. Enyedy, “Interaction of anticancer reduced Schiff base coumarin derivatives with human serum albumin investigated by fluorescence quenching and molecular modeling,” Bioorganic Chemistry, vol. 52, pp. 16–23, 2014. View at Publisher · View at Google Scholar · View at Scopus
  60. H. F. Crouse, E. M. Petrunak, A. M. Donovan, A. C. Merkle, B. L. Swartz, and S. Basu, “Static and dynamic quenching of tryptophan fluorescence in various proteins by a chromium (III) complex,” Spectroscopy Letters, vol. 44, no. 5, pp. 369–374, 2011. View at Publisher · View at Google Scholar · View at Scopus
  61. D. Wu, B. Du, H. Ma, Q. Wei, and G. Xu, “Quenching of the intrinsic fluorescence of human serum albumin by trimethoxyphenylfluorone-Mo(VI) complex,” Spectroscopy Letters, vol. 39, no. 4, pp. 399–408, 2006. View at Publisher · View at Google Scholar · View at Scopus
  62. K.-I. Sugae and B. Jirgensons, “Amino acid sequence next to tryptophan in human and bovine serum albumin,” Journal of Biochemistry, vol. 56, no. 5, pp. 457–464, 1964. View at Google Scholar · View at Scopus
  63. A. A. Rhodes, B. L. Swartz, E. R. Hosler et al., “Static quenching of tryptophan fluorescence in proteins by a dioxomolybdenum(VI) thiolate complex,” Journal of Photochemistry and Photobiology, vol. 293, pp. 81–87, 2014. View at Publisher · View at Google Scholar · View at Scopus
  64. Q. Wei, D. Wu, B. Du, Y. Li, and C. Duan, “Interaction of m-nitrophenylfluorone-Mo(VI) complex as a probe with human serum albumin: a fluorescence quenching study,” Spectrochimica Acta—Part A: Molecular and Biomolecular Spectroscopy, vol. 63, no. 3, pp. 532–535, 2006. View at Publisher · View at Google Scholar · View at Scopus
  65. H. Wu, S. Lian, Y. Shen, and Y. Wan, “Interactions of lysozyme with 6-amino-4-aryl-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine-5-carbonitriles: a fluorescence quenching study,” Analytical Sciences, vol. 23, no. 4, pp. 419–422, 2007. View at Publisher · View at Google Scholar · View at Scopus
  66. S. H. Laurie and D. E. Pratt, “A spectroscopie study of nickel(II)-bovine serum albumin binding and reactivity,” Journal of Inorganic Biochemistry, vol. 28, no. 4, pp. 431–439, 1986. View at Publisher · View at Google Scholar · View at Scopus
  67. C.-Q. Jiang, M.-X. Gao, and J.-X. He, “Study of the interaction between terazosin and serum albumin: synchronous fluorescence determination of terazosin,” Analytica Chimica Acta, vol. 452, no. 2, pp. 185–189, 2002. View at Publisher · View at Google Scholar · View at Scopus