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BioMed Research International
Volume 2014, Article ID 872701, 6 pages
http://dx.doi.org/10.1155/2014/872701
Research Article

Morphological Analysis and Interaction of Chlorophyll and BSA

Grupo de Materiais Nanoestruturados, Universidade Federal de Mato Grosso, 78600-000 Barra do Garças, MT, Brazil

Received 27 February 2014; Revised 21 April 2014; Accepted 21 April 2014; Published 18 May 2014

Academic Editor: Rumiana Koynova

Copyright © 2014 Filipe D. S. Gorza 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. R. E. Olson and D. D. Christ, “Plasma protein binding of drugs,” Annual Reports in Medicinal Chemistry, vol. 31, pp. 327–336, 1996. View at Publisher · View at Google Scholar
  2. H. A. Tajmir-Riahi, “An overview of drug binding to human serum albumin: protein folding and unfolding,” Scientia Iranica, vol. 14, no. 2, pp. 87–95, 2007. View at Google Scholar · View at Scopus
  3. A. A. Ouameur, R. Marty, and H. A. Tajmir-Riahi, “Human serum albumin complexes with chlorophyll and chlorophyllin,” Biopolymers, vol. 77, no. 3, pp. 129–136, 2005. View at Publisher · View at Google Scholar · View at Scopus
  4. Q. Yang, X. Zhou, and X. Chen, “Combined molecular docking and multi-spectroscopic investigation on the interaction between Eosin B and human serum albumin,” Journal of Luminescence, vol. 131, no. 4, pp. 581–586, 2011. View at Publisher · View at Google Scholar · View at Scopus
  5. M. Bardhan, J. Chowdhury, and T. Ganguly, “Investigations on the interactions of aurintricarboxylic acid with bovine serum albumin: steady state/time resolved spectroscopic and docking studies,” Journal of Photochemistry and Photobiology B: Biology, vol. 102, no. 1, pp. 11–19, 2011. View at Publisher · View at Google Scholar · View at Scopus
  6. Y. Li, Y. Ge, Y. Zhang et al., “Interaction of coomassie brilliant blue G250 with human serum albumin: probing of the binding mechanism and binding site by spectroscopic and molecular modeling methods,” Journal of Molecular Structure, vol. 968, no. 1–3, pp. 24–31, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. P. Daneshgar, A. A. Moosavi-Movahedi, P. Norouzi, M. R. Ganjali, A. Madadkar-Sobhani, and A. A. Saboury, “Molecular interaction of human serum albumin with paracetamol: spectroscopic and molecular modeling studies,” International Journal of Biological Macromolecules, vol. 45, no. 2, pp. 129–134, 2009. View at Publisher · View at Google Scholar · View at Scopus
  8. J. Wang, S. Li, X. Peng et al., “Multi-spectroscopic studies on the interaction of human serum albumin with astilbin: binding characteristics and structural analysis,” Journal of Luminescence, vol. 136, pp. 422–429, 2013. View at Publisher · View at Google Scholar
  9. N. C. de Souza, J. C. J. Flores, and J. R. Silva, “Layer-by-layer films from tartrazine dye with bovine serum albumin,” Chemical Physics Letters, vol. 484, no. 1–3, pp. 33–36, 2009. View at Publisher · View at Google Scholar · View at Scopus
  10. N. Dash, A. Mishra, and G. Krishnamoorthy, “Alkyl chain dependent interactions of ligands with bovine serum albumin,” Journal of Pharmaceutical and Biomedical Analysis, vol. 77, pp. 55–62, 2013. View at Publisher · View at Google Scholar
  11. R. Huang, S. Zhang, L. Pan, J. Li, F. Liu, and H. Liu, “Spectroscopic studies on the interactions between imidazolium chloride ionic liquids and bovine serum albumin,” Spectrochimica Acta A: Molecular AndBiomolecular Spectroscopy, vol. 104, pp. 377–382, 2013. View at Publisher · View at Google Scholar
  12. J. H. Shi, Y. Y. Zhu, J. Wang, J. Chen, and Y. J. Shen, “Intermolecular interaction of prednisolone with bovine serum albumin: spectroscopic and molecular docking methods,” Spectrochimica Acta A: Molecular and Biomolecular Spectroscopy, vol. 103, pp. 287–294, 2013. View at Publisher · View at Google Scholar
  13. S. Nafisi, G. Bagheri Sadeghi, and A. Panahyab, “Interaction of aspirin and vitamin C with bovine serum albumin,” Journal of Photochemistry and Photobiology B: Biology, vol. 105, no. 3, pp. 198–202, 2011. View at Publisher · View at Google Scholar · View at Scopus
  14. P. N. P. Bourassa, C. D. Kanakis, P. Tarantilis, M. G. Pollissiou, and H. A. Tajmir-Riahi, “Resveratrol, genistein, and curcumin bind bovine serum albumin,” Journal of Physical Chemistry B, vol. 114, no. 9, pp. 3348–3354, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. S. P. Mitra, “Binding and stability of curcumin in presence of bovine serum albumin,” Journal of Surface Science and Technology, vol. 23, no. 3-4, pp. 91–110, 2007. View at Google Scholar · View at Scopus
  16. Barik, K. I. Priyadarsini, and H. Mohan, “Photophysical studies on binding of curcumin to bovine serum albumin,” Photochemistry and Photobiology, vol. 77, no. 6, pp. 597–603, 2003. View at Publisher · View at Google Scholar
  17. Y. Zhang, B. Zhou, X. Zhang, P. Huang, C. Li, and Y. Liu, “Interaction of malachite green with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods,” Journal of Hazardous Materials, vol. 163, no. 2-3, pp. 1345–1352, 2009. View at Publisher · View at Google Scholar · View at Scopus
  18. J. Sereikaite, Z. Bumeliene, and V.-A. Bumelis, “Bovine serum albumin-dye binding,” Acta Chromatographica, no. 15, pp. 298–307, 2005. View at Google Scholar · View at Scopus
  19. S. Bakkialakshmi and D. Chandrakala, “A spectroscopic investigations of anticancer drugs binding to bovine serum albumin,” Spectrochimica Acta A: Molecular and Biomolecular Spectroscopy, vol. 88, pp. 2–9, 2012. View at Publisher · View at Google Scholar · View at Scopus
  20. T. Hattori, K. Kimura, E. Seyrek, and P. L. Dubin, “Binding of bovine serum albumin to heparin determined by turbidimetric titration and frontal analysis continuous capillary electrophoresis,” Analytical Biochemistry, vol. 295, no. 2, pp. 158–167, 2001. View at Publisher · View at Google Scholar · View at Scopus
  21. R. R. G. Maciel, A. A. de Almeida, O. G. C. Godinho et al., “Ascorbic acid and BSA protein in solution and films: interaction and surface morphological structure,” BioMed Research International, vol. 2013, Article ID 461365, 7 pages, 2013. View at Publisher · View at Google Scholar
  22. H. Shibata, H. Ochiai, T. Kawashima, T. Okamoto, and I. Inamura, “Preparation and properties of the water-soluble chlorophyll-bovine serum albumin complexes,” BBA—Bioenergetics, vol. 852, no. 2-3, pp. 175–182, 1986. View at Google Scholar · View at Scopus
  23. S. W. Kimm and S. C. Park, “Evidences for the existence of antimutagenic factors in edible plants,” Korean Journal of Biochemistry, vol. 14, no. 2, pp. 47–59, 1982. View at Google Scholar · View at Scopus
  24. T. Ong, W. Z. Whong, J. Stewart, and H. E. Brockman, “Chlorophyllin: a potent antimutagen against environmental and dietary complex mixtures,” Mutation Research, vol. 173, no. 2, pp. 111–115, 1986. View at Google Scholar · View at Scopus
  25. M. G. Ferruzzi, V. Böhm, P. D. Courtney, and S. J. Schwartz, “Antioxidant and antimutagenic activity of dietary chlorophyll derivatives determined by radical scavenging and bacterial reverse mutagenesis assays,” Journal of Food Science, vol. 67, no. 7, pp. 2589–2595, 2002. View at Google Scholar · View at Scopus
  26. G. C. Bez, B. Q. Jordão, V. E. P. Vicentini, and M. S. Mantovani, “Investigation of genotoxic and antigenotoxic activities of chlorophylls and chlorophyllin in cultured V79 cells,” Mutation Research—Genetic Toxicology and Environmental Mutagenesis, vol. 497, no. 1-2, pp. 139–145, 2001. View at Publisher · View at Google Scholar · View at Scopus
  27. B. M. Dorvigny, L. M. S. Perera, S. D. Aguirre et al., “Healing effect of Pinus caribaea var. caribaea paste on aseptic open wounds,” Revista Cubana de Plantas Medicinales, vol. 16, no. 1, pp. 24–33, 2011. View at Google Scholar · View at Scopus
  28. C. A. Schneider, W. S. Rasband, and K. W. Eliceiri, “NIH Image to Image J: 25 years of image analysis,” Nature Methods, vol. 9, no. 7, pp. 671–675, 2012. View at Google Scholar
  29. D. Gao, Y. Tian, F. Liang et al., “Investigation on the pH-dependent binding of Eosin Y and bovine serum albumin by spectral methods,” Journal of Luminescence, vol. 127, no. 2, pp. 515–522, 2007. View at Publisher · View at Google Scholar · View at Scopus
  30. M. C. Petty, Langmuir-Blodgett Films: An Introduction, Cambridge University Press, 1st edition, 1996.
  31. J. B. Brito, D. J. C. Gomes, V. D. Justina et al., “Nanostructured films from phthalocyanine and carbon nanotubes: surface morphology and electrical characterization,” Journal of Colloid and Interface Science, vol. 367, no. 1, pp. 467–471, 2012. View at Publisher · View at Google Scholar · View at Scopus
  32. P. Daneshegar, A. A. Moosavi-Movahedi, P. Norouzi, M. R. Ganjali, M. Farhadic, and N. Sheibani, “Characterization of paracetamol binding with normal and glycated human serum albumin assayed by a new electrochemical method,” Journal of the Brazilian Chemical Society, vol. 23, no. 2, pp. 315–321, 2012. View at Publisher · View at Google Scholar · View at Scopus
  33. R. S. Kumar, P. Paul, A. Riyasdeen et al., “Human serum albumin binding and cytotoxicity studies of surfactant-cobalt(III) complex containing 1,10-phenanthroline ligand,” Colloids and Surfaces B: Biointerfaces, vol. 86, no. 1, pp. 35–44, 2011. View at Publisher · View at Google Scholar · View at Scopus
  34. I. D. Kuntz Jr., F. P. Gasparro, M. D. Johnston Jr., and R. P. Taylor, “Molecular interactions and the Benesi-Hildebrand equation,” Journal of the American Chemical Society, vol. 90, no. 18, pp. 4778–4781, 1968. View at Publisher · View at Google Scholar · View at Scopus
  35. K. A. Connors, Binding Constants: The Measurement of Molecular Complex Stability, Wiley-Interscience, New York, NY, USA, 1st edition, 1987.
  36. S. Naveenraj and S. Anandan, “Binding of serum albumins with bioactive substances—nanoparticles to drugs,” Journal of Photochemistry and Photobiology C: Photochemistry Reviews, vol. 14, pp. 53–71. View at Publisher · View at Google Scholar
  37. A. L. Barabási and H. E. Stanley, Fractal Concepts in Surface Growth, Cambridge University Press, 1st edition, 1995.
  38. N. C. de Souza, J. R. Silva, C. A. Rodrigues, L. D. F. Costa, J. A. Giacometti, and O. N. Oliveira Jr., “Adsorption processes in layer-by-layer films of poly(o-methoxyaniline): the role of aggregation,” Thin Solid Films, vol. 428, no. 1-2, pp. 232–236, 2003. View at Publisher · View at Google Scholar · View at Scopus
  39. L. Ottaviano, P. Parisse, V. Grossi, and M. Passacantando, “Nanowire directed diffusion limited aggregation growth of nanoparticles,” Journal of Non-Crystalline Solids, vol. 356, no. 37–40, pp. 2076–2078, 2010. View at Publisher · View at Google Scholar · View at Scopus
  40. T. A. Witten Jr. and L. M. Sander, “Diffusion-limited aggregation, a kinetic critical phenomenon,” Physical Review Letters, vol. 47, no. 19, pp. 1400–1403, 1981. View at Publisher · View at Google Scholar · View at Scopus