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Bioinorganic Chemistry and Applications
Volume 2014, Article ID 325873, 8 pages
http://dx.doi.org/10.1155/2014/325873
Research Article

Inhibitory Effect of Curcumin-Cu(II) and Curcumin-Zn(II) Complexes on Amyloid-Beta Peptide Fibrillation

Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667, India

Received 15 May 2014; Revised 8 July 2014; Accepted 9 July 2014; Published 23 July 2014

Academic Editor: Igor O. Fritsky

Copyright © 2014 Rona Banerjee. 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. I. Chattopadhyay, K. Biswas, U. Bandyopadhyay, and R. K. Banerjee, “Turmeric and curcumin: biological actions and medicinal applications,” Current Science, vol. 87, no. 1, pp. 44–53, 2004. View at Google Scholar · View at Scopus
  2. A. K. Singh, A. Gupta, A. K. Mishra, V. Gupta, P. Bansal, and S. Kumar, “Medicinal plant for curing Alzheimer's disease,” International Journal of Pharmaceutical & Biological Archive, vol. 1, pp. 108–114, 2010. View at Google Scholar
  3. B. Zhao, “Natural antioxidants for neurodegenerative diseases,” Molecular Neurobiology, vol. 31, no. 1–3, pp. 283–293, 2005. View at Publisher · View at Google Scholar
  4. F. Dajas, A. Rivera-Megret, F. Blasina et al., “Neuroprotection by flavonoids,” Brazilian Journal of Medical and Biological Research, vol. 36, no. 12, pp. 1613–1620, 2003. View at Publisher · View at Google Scholar · View at Scopus
  5. I. Häke, S. Schönenberger, J. Neumann et al., “Neuroprotection and enhanced neurogenesis by extract from the tropical plant Knema laurina after inflammatory damage in living brain tissue,” Journal of Neuroimmunology, vol. 206, no. 1-2, pp. 91–99, 2009. View at Publisher · View at Google Scholar · View at Scopus
  6. M. Ahmed, J. Davis, D. Aucoin et al., “Structural conversion of neurotoxic amyloid-Β 1-42 oligomers to fibrils,” Nature Structural and Molecular Biology, vol. 17, no. 5, pp. 561–567, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. V. V. Tõugu, A. Tiiman, and P. Palumaa, “Interactions of Zn(ii) and Cu(ii) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity,” Metallomics, vol. 3, no. 3, pp. 250–261, 2011. View at Publisher · View at Google Scholar · View at Scopus
  8. M. E. McLellan, S. T. Kajdasz, B. T. Hyman, and B. J. Bacskai, “In vivo imaging of reactive oxygen species specifically associated with thioflavine S-positive amyloid plaques by multiphoton microscopy,” Journal of Neuroscience, vol. 23, no. 6, pp. 2212–2217, 2003. View at Google Scholar · View at Scopus
  9. V. Chauhan, L. Ji, and A. Chauhan, “Anti-amyloidogenic, anti-oxidant and anti-apoptotic role of gelsolin in Alzheimer's disease,” Biogerontology, vol. 9, no. 6, pp. 381–389, 2008. View at Publisher · View at Google Scholar · View at Scopus
  10. V. Tõugu, A. Karafin, and P. Palumaa, “Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-β peptide,” Journal of Neurochemistry, vol. 104, no. 5, pp. 1249–1259, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. L. Ghalebani, A. Wahlstrom, J. Danielsson, S. K. T. S. Warmlander, and A. Graslund, “pH-dependence of the specific binding of Cu(II) and Zn(II) ions to the amyloid-β peptide,” Biochemical and Biophysical Research Communications, vol. 421, no. 3, pp. 554–560, 2012. View at Publisher · View at Google Scholar
  12. L. Baum and A. Ng, “Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer's disease animal models,” Journal of Alzheimer's Disease, vol. 6, no. 4, pp. 367–377, 2004. View at Google Scholar
  13. P. Anand, S. G. Thomas, A. B. Kunnumakkara et al., “Biological activities of curcumin and its analogues (Congeners) made by man and Mother Nature,” Biochemical Pharmacology, vol. 76, no. 11, pp. 1590–1611, 2008. View at Publisher · View at Google Scholar · View at Scopus
  14. Y. Song, J. Xu, L. Ding, Q. Hou, J. Liu, and Z. Zhu, “Syntheses, characterization and biological activities of rare earth metal complexes with curcumin and 1,10-phenanthroline-5,6-dione,” Journal of Inorganic Biochemistry, vol. 103, no. 3, pp. 396–400, 2009. View at Publisher · View at Google Scholar
  15. A. Barik, B. Mishra, L. Shen et al., “Evaluation of a new copper(II)-curcumin complex as superoxide dismutase mimic and its free radical reactions,” Free Radical Biology and Medicine, vol. 39, no. 6, pp. 811–822, 2005. View at Publisher · View at Google Scholar · View at Scopus
  16. X. Mei, D. Xu, S. Xu, and Y. Zheng, “Novel role of Zn(II)-curcumin in enhancing cell proliferation and adjusting proinflammatory cytokine-mediated oxidative damage of ethanol-induced acute gastric ulcers,” Chemico-Biological Interactions, vol. 197, no. 1, pp. 31–39, 2012. View at Publisher · View at Google Scholar
  17. F. Yang, G. P. Lim, A. N. Begum et al., “Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo,” Journal of Biological Chemistry, vol. 280, no. 7, pp. 5892–5901, 2005. View at Publisher · View at Google Scholar · View at Scopus
  18. X. Zhao, T. Jiang, L. Wang, H. Yang, S. Zhang, and P. Zhou, “Interaction of curcumin with Zn(II) and Cu(II) ions based on experiment and theoretical calculation,” Journal of Molecular Structure, vol. 984, no. 1–3, pp. 316–325, 2010. View at Publisher · View at Google Scholar · View at Scopus
  19. B. Zebib, Z. Mouloungui, and V. Noirot, “Stabilization of curcumin by complexation with divalent cations in glycerol/water system,” Bioinorganic Chemistry and Applications, vol. 2010, Article ID 292760, 8 pages, 2010. View at Publisher · View at Google Scholar
  20. A. Barik, B. Mishra, A. Kunwar et al., “Comparative study of copper(II)-curcumin complexes as superoxide dismutase mimics and free radical scavengers,” European Journal of Medicinal Chemistry, vol. 42, no. 4, pp. 431–439, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. M. I. Khalil, A. M. Al-Zahem, and M. H. Al-Qunaibit, “Synthesis, characterization, Mössbauer parameters, and antitumor activity of Fe(III) curcumin complex,” Bioinorganic Chemistry and Applications, vol. 2013, Article ID 982423, 5 pages, 2013. View at Publisher · View at Google Scholar
  22. P. Malik and T. K. Mukherjee, “Structure-function elucidation of antioxidative and prooxidative activities of the polyphenolic compound curcumin,” Chinese Journal of Biology, vol. 2014, Article ID 396708, 8 pages, 2014. View at Publisher · View at Google Scholar
  23. I. A. Mastrangelo, M. Ahmed, T. Sato et al., “High-resolution atomic force microscopy of soluble Aβ42 oligomers,” Journal of Molecular Biology, vol. 358, no. 1, pp. 106–119, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. B. Anindya, S. Alok, B. N. Kaur, M. Jassal, and M. Prosenjit, “Curcumin and curcumin-metal complex: ancient weapon, modern targets,” Universal Journal of Pharmacy, vol. 2, pp. 8–19, 2013. View at Google Scholar
  25. J. R. Lou, X. Zhang, J. Zheng, and W. Ding, “Transient metals enhance cytotoxicity of curcumin: potential involvement of the NF-κB and mTOR signaling pathways,” Anticancer Research, vol. 30, pp. 3249–3256, 2010. View at Google Scholar
  26. M. A. Addicoat, G. F. Metha, and T. W. Kee, “Density functional theory investigation of Cu(I)- and Cu(II)-curcumin complexes,” Journal of Computational Chemistry, vol. 32, no. 3, pp. 429–438, 2011. View at Publisher · View at Google Scholar · View at Scopus