An investigation of the molecular interactions of diacetylcurcumin with Ribonuclease A

Protein and Peptide Letters

Volumn 16, Issue 12, 2009, Pages 1485-1495

  Sahoo, Bijaya Ketan ^a   Ghosh, Kalyan Sundar ^b   Dasgupta, Swagata ^c  

^a MITS Engineering College   (India)

^b STATE UNIVERSITY OF NEW YORK   (United States)

^c INDIAN INSTITUTE OF TECHNOLOGY   (India)

Author keywords

Binding; CD; Diacetylcurcumin; Docking; Fluorescence; FTIR; Ribonuclease A

Indexed keywords

CURCUMIN; DIACETYLCURCUMIN; DRUG DERIVATIVE; LIGAND; PANCREATIC RIBONUCLEASE;

ARTICLE; BINDING SITE; CHEMISTRY; METABOLISM;

BINDING SITES; CURCUMIN; LIGANDS; RIBONUCLEASE, PANCREATIC;

EID: 73449132943     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609789839278     Document Type: Article

References (68)

1. Govindarajan, V. S. Turmeric. Chemistry, technology, and quality, CRC Crit. Rev. Food Sci. Nutr., 1980, 12 (8), 199-301.
2. Dickinson, D. A.; Levonen, A. L.; Moellering, D. R.; Arnold, E. K.; Zhang, H.; Darley-Usmar, V. M.; Forman, H. J. Human glutamate cysteine ligase gene regulation through the electrophile response element. Free Radical Biol. M ed., 2004, 37 (8), 1152-1159.
3. Ruby, A. J.; Kuttan, G.; Dinesh Babu, K.; Rajasekharan, K. N.; Kuttan, R. Anti-tumour and antioxidant activity of natural curcuminoids. Cancer Lett., 1995, 94 (1), 79-83.
4. Aggarwal, B. B.; Kumar, A.; Bharti, A. C. Anticancer potential of curcumin: preclinical and clinical studies. Anticancer Res., 2003, 23 (1), 363-398.
5. Egan, M. E.; Pearson, M.; Weiner, S. A.; Rajendran, V.; Rubin, D.; Glökner-Pagel, J.; Canny, S.; Du, K.; Lukacs, G. L.; Caplan, M. J. Curcumin, a Major Constituent of Turmeric, Corrects Cystic Fibrosis Defects. Science, 2004, 304, 600-602.
6. Skrzypezac-Jankun, E.; McCabe, N. P.; Selman, S. H.; Jankun, J. Curcumin inhibits lipoxygenase by binding to its central cavity: Theoretical and X-ray evidence. Int. J. Mol. M ed., 2000, 6 (5), 521-526.
7. Sreejayan, N.; Priyadarsini, K. I.; Devasagayam, T. P. A.; Rao, M. N. A. Inhibition of radiation-induced lipid peroxidation by curcumin. Int. J. Pharm., 1997, 151 (1), 127-130.
8. Joe, B.; Vijaykumar, M.; Lokesh, B. R. Biological Properties of Curcumin-Cellular and Molecular Mechanisms of Action Crit. Rev. Food. Sci. Nutr., 2004, 44 (2), 97-111.
9. Cui, L.; Miao, J.; Cui, L. Cytotoxic effect of curcumin on malaria parasite plasmodium falciparum: inhibition of histone acetylation and generation of reactive oxygen species. Antimicrob. Agents Chemother., 2007, 51 (2), 488-494.
10. Gafner, S.; Lee, S-K.; Cuendet, M.; Barthélémy, S.; Vergnes, L.; Labidalle, S.; Mehta, R. G.; Boone, C. W.; Pezzuto, J. M. Biologic evaluation of curcumin and structural derivatives in cancer chemoprevention model systems, Phytochem., 2004, 65 (21), 2849.
11. Aggarwal, B. B.; Bhatt, I. D.; Ichikawa, H.; Ahn, K. S.; Sethi, G.; Sandur, S. K.; Sundaram, C.; Seeram, N.; Shishodia, S. Curcuminbiological and medicinal properties, in Turmeric the Genus Curcuma, by Ravindran, P. N., Babu, K. N., Sivaraman, K. (Eds.), New York, CRC Press, 297-368, 2007.
12. Mishra, S.; Narain, U.; Mishra, R.; Misra, K. Design, development and synthesis of mixed bioconjugates of piperic acid-glycine, curcumin-glycine/ alanine and curcumin-glycine-piperic acid and their antibacterial and antifungal properties, Bioorg. Med. Chem., 2005, 13 (5), 1477-1486.
13. Sumanont, Y.; Murakami, Y.; Tohda, M.; Vajragupta, O.; Matsumoto, K.; Watanabe, H. Evaluation of the nitric oxide radical scavenging activity of manganese complexes of curcumin and its derivative. Biol. Pharm. Bull., 2004, 27 (2), 170-173.
14. Sumanont, Y.; Murakami, Y.; Tohda, M.; Vajragupta, O.; Watanabe H.; Matsumoto, K. Prevention of kainic acid-induced changes in nitric oxide level and neuronal cell damage in the rat hippocampus by manganese complexes of curcumin and diacetylcurcumin. Life Sci., 2006, 78 (16), 1884-1891.
15. Vajragupta, O.; Boonchoong, P.; Watanabe, H.; Tohda, M.; Kummasud, N.; Sumanont, Y. Manganese complexes of curcumin and its derivatives: evaluation for the radical scavenging ability and neuroprotective activity. Free Radical Biol. M ed., 2003, 35 (12), 1632-1644.
16. Vajragupta, O.; Boonchoong, P.; Berliner, L. J. Manganese complexes of curcumin analogues: evaluation of hydroxyl radical scavenging ability, superoxide dismutase activity and stability towards hydrolysis. Free Radical Res., 2004, 38 (3), 303-314.
17. Borsari, M.; Ferrari, E.; Grandi, R.; Saladini, M. Curcuminoids as potential new iron-chelating agents: spectroscopic, polarographic and potentiometric study on their Fe (III) complexing ability. Inorg. Chim. Acta., 2002, 328 (1), 61-68.
18. Deters, M.; Knochenwefel, H.; Lindhorst, D.; Koal, T.; Meyer, H. H.; Hänsel, W.; Resch, K.; Kaever, V. Different curcuminoids inhibit T-Lymphocyte proliferation independently of their radical scavenging activities, Pharm. Res., 2008, 25 (8), 1822-1827.
19. Mishra, S.; Karmodiya, K.; Surolia, N.; Surolia, A. Synthesis and exploration of novel curcumin analogues as anti-malarial agents. Bioorg. Med. Chem., 2008, 16 (6), 2894-2902.
20. Douglas, D. E. 4, 4'-Diacetyl curcumin-in-vitro histamine-blocking activity, J. Pharm. Pharmacol., 1993, 45 (8), 766.
21. Basile, V.; Ferrari, E.; Lazzari, S.; Belluti, S.; Pignedoli, F.; Imbriano, C. Curcumin derivatives: Molecular basis of their anti-cancer activity. Biochem. Pharmacol. 2009, doi:10.1016/j. bcp. 2009. 06.105
22. Shoba, G.; Joy, D.; Joseph, T.; Majeed, M.; Rajendran, R.; Srinivas, P. S. Influence of piperine on the pharmacokinetics of curcumin in animals and human volunteers. Planta M ed., 1998, 64 (4), 353-356.
23. Mishra, S.; Narain, U.; Mishra, R.; Misra, K. Design, development and synthesis of mixed bioconjugates of piperic acid-glycine, curcumin-glycine/ alanine and curcumin-glycine-piperic acid and their antibacterial and antifungal properties. Bioorg. Med. Chem., 2005, 13 (5), 1477-1486.
24. Cuchillo, C. M.; Vilanova, M.; Nogués, M. V. in Ribonucleases: Structures and Functions (D'Alessio, G., Riordan, J. F., Ed). Academic Press, New York. 1997, pp. 271-304.
25. Raines, R. T. Ribonuclease A. Chem. Rev., 1998, 98 (3), 1045-1066.
26. Folkman, J.; Klagsbrun, M. Angiogenic factors. Science, 1987, 235, 442-447.
27. Riordan, J. F. in Ribonucleases: Structures and Functions (D'Alessio, G., Riordan, J. F., Ed). Academic Press, New York. 1997, pp. 445-489.
28. Fett, J. W.; Strydom, D. J.; Lobb, R. R.; Alderman, E. M.; Bethune, J. L.; Riordan, J. F.; Vallee, B. L. Isolation and characterization of angiogenin, an angiogenic protein from human carcinoma cells. Biochemistry, 1985, 24 (20), 5480-5486.
29. Sorrentino, S.; Glitz, G.; Hamann, J.; Loegering, A.; Checkel, L.; Gleich, G. J. Eosinophil-derived neurotoxin and human liver ribonuclease. Identity of structure and linkage of neurotoxicity to nuclease activity. J. Biol. Chem., 1992, 267 (21), 14859-14865.
30. D'Alessio, G.; Di Donato, A.; Mazzarella, L.; Piccoli, R. Seminal ribonuclease: the importance of diversity, in Ribonucleases Structures and Functions, by D'Alessio, G. and Riordan, J. F. (Eds.), New York, Academic Press, pp. 383-423. 1997.
31. Gleich, G. J.; Loegering, D. A.; Bell, M. P.; Checkel, J. L.; Ackerman, S. J.; McKean, D. J. Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease. Proc. Natl. Acad. Sci., 1986, 83 (10), 3146-3150.
32. Sahoo, B. K.; Ghosh, K. S.; Bera, R.; Dasgupta, S. Studies on the interaction of diacetylcurcumin with calf thymus-DNA. Chem. Phys., 2008, 351 (1-3), 163-169.
33. Sahoo, B. K.; Ghosh, K. S.; Dasgupta, S. Investigating the binding of curcumin derivatives to bovine serum albumin. Biophys. Chem., 2008, 132 (2-3), 81-88.
34. Roughley, P. J.; Whiting, D. A. Experiments in the Biosynthesis of Curcumin. J. Chem. Soc. Perkin Trans., 1973, 1, 2379-2388.
35. Sela, M.; Anfinsen, C. B. Some spectrophotometric and polarimetric experiments with ribonuclease. Biochim. Biophys. Acta, 1957, 24, 229-235.
36. Lakowicz, J. R. Principles of Fluorescence Spectroscopy. Springer, New York, 2006.
37. Byler, D. M.; Susi, H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 1986, 25 (3), 469-487.
38. Dong, A. C.; Huang, P.; Caughey, W. S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry, 1990, 29 (13), 3303-3308.
39. Susi, H.; Byler, D. M. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol., 1986, 130, 290-311.
40. Berman, H. M.; Westbrook, J.; Feng, Z.; Gilliland, G.; Bhat, T. N.; Weissig, H.; Shindyalov, I. N.; Bourne, P. E. The Protein Data Bank. Nucleic Acids Res., 2000, 28 (1), 235-242.
41. Rarey, M.; Kramer, B.; Lengauer, T.; Klebe, G. A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol., 1996, 261 (3), 470-489.
42. DeLano, W. L. The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos CA, USA. 2006, http://pymol. sourceforge.net/
43. Han, L. Y.; Lin, H. H.; Li, Z. R.; Zheng, C. J.; Cao, Z. W.; Xie, B.; Chen, Y. Z. PEARLS: program for energetic analysis of receptorligand system, J. Chem. Inf. Model, 2006, 46 (1), 445-450.
44. Hubbard, S. J.; Thornton, J. M. 'NACCESS'. Computer Program, Department of Biochemistry and Molecular Biology, University College, London, 1993.
45. Zsila, F.; Bikádi, Z.; Simonyi, M. Molecular basis of the Cotton effects induced by the binding of curcumin to human serum albumin, Tetrahedron: Asymmetry, 2003, 14 (16), 2433-2444.
46. Benesi, H. A.; Hildebrand, J. H. A Spectrophotometric Investigation of the Interaction of Iodine with Aromatic Hydrocarbons. J. Am. Chem. Soc., 1949, 71 (8), 2703-2707.
47. Scatchard, G. The attractions of proteins for small molecules and ions. Ann. N. Y. Acad. Sci., 1949, 51 (4), 660-672.
48. Congdon, R. W.; Muth, G. W.; Splittgerber, A. G. The Binding Interaction of Coomassie Blue with Proteins. Anal. Biochem., 1993, 213 (2), 407-413.
49. Lakowicz, J. R.; Weber, G. Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry, 1973, 12 (21), 4171-4179.
50. Weber, G.; Young, L. B. Fragmentation of bovine serum albumin by pepsin. I: Origin of the acid expansion of the albumin molecule. J. Biol. Chem., 1964, 239 (5), 1415-1423.
51. Ward, L. D. Measurement of ligand binding to proteins by fluorescence spectroscopy, Methods Enzymol., 1985, 117, 400-414.
52. Clegg, R. M. in Fluorescence imaging spectroscopy and microscopy (Wang, X. F., Herman, B., Ed.). pp. 179-252. John Wiley & Sons, New York. 1996.
53. 2+ transport ATPase molecules in artificial membranes. Biochemistry, 1977, 16, 1262-1267.
54. Yuan, T.; Weljie, A. M.; Vogel, H. J. Tryptophan Fluorescence Quenching by Methionine and Selenomethionine Residues of Calmodulin: Orientation of Peptide and Protein Binding. Biochemistry, 1998, 37 (9), 3187-3195.
55. Yuan, J. L.; Iv, Zhong; Liu, Z. G.; Hu, Z.; Zou, G. L. Study on interaction between apigenin and human serum albumin by spectroscopy and molecular modeling. J. Photochem. Photobiol. A, 2007, 191 (2-3), 104-113.
56. Wang, Y. Q.; Zhang H. M.; Zhang G. C. Studies of the interaction between palmatine hydrochloride and human serum albumin by fluorescence quenching method J. Pharm. Biomed. Anal., 2006, 41 (3), 1041-1046.
57. Gore, M. G. Spectrophotometry and Spectrofluorimetry: A Practical approach. Oxford University Press, New York, 2000.
58. Hong, G.; Lei, L.; Liu, J.; Kong, Q.; Chen, X.; Hu, Z. The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectrophotometric methods. J. Photochem. Photobiol., A, 2004, 167 (2-3), 213-221.
59. Wlodawar, A.; Borkakoti, N.; Moss, D. S.; Howlin, B. Comparison of two independently refined models of ribonuclease-A. Acta Crystallogr., 1986, B42 (4), 379-387.
60. Neault, J. F.; Ragi, C.; Novetta-Dellen, A.; Tajmir-Riahi, H. A. Aspirin interaction with ribonuclease a. Cell Biochem. Biophys., 2006, 46 (1), 27-33.
61. Gaudreau, S.; Novetta-dellen, A.; Neault, J. F.; Diamantoglou, S.; Tajmir-riahi, H. A. 3'-Azido-3'-deoxythymidine binding to ribonuclease A: Model for drug-protein interaction, Biopolymers, 2003, 72 (6), 435-441.
62. Neault, J. F.; Diamantoglou, S.; Beauregard, M.; Nafisi, Sh.; Tajmir-Riahi, H. A. Protein Unfolding in Drug-RNase Complexes. J. Biomol. Struct. Dyn., 2008, 25 (4), 387-394.
63. N'soukpoé-Kossi, C. N.; Ragi, C.; Tajmir-Riahi, H. A. RNase A - tRNA binding alters protein conformation. Biochem. Cell Biol., 2007, 85 (3), 311-318.
64. Omenn, G. S.; Ctjatrecasas, P.; Anfinsen, C. B. Studies of the Aromatic Circular Dichroism of Staphylococcal Nuclease. Proc. Nat. Acad. Sci., 1969, 64 (3), 923-930.
65. Horwitz, J.; Strickland, E. H.; Billups, C. Analysis of the vibrational structure in the near-ultraviolet circular dichroism and absorption spectra of tyrosine derivatives and ribonuclease-A at 77.deg. K. J. Am. Chem. Soc., 1970, 92 (7), 2119.
66. Simona, D.; Stelea, P. P.; Albert, S. B.; Timothy, A. K. Thermal unfolding of ribonuclease A in phosphate at neutral pH: Deviations from the two-state model. Protein Sci., 2001, 10 (5), 970.
67. delCardayré, S. B.; Ribó, M.; Yokel, E. M.; Quirk, D. J.; Rutter, J.; Raines, R. T. Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln 11. Protein Eng., 1995, 8 (3), 261-273.
68. Nogués, M. V.; Vilanova, M.; Cuchillo, C. M. Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites. Biochim. Biophys. Acta, 1995, 1253 (1), 16-24.