Biological Evaluation of a New Synthesized Pt(II) Complex by Cytotoxic and Spectroscopic Studies

Cell Biochemistry and Biophysics

Volumn 71, Issue 3, 2015, Pages 1415-1424

  Divsalar, Adeleh ^a   Razmi, Mahdieh ^a   Saboury, Ali Akbar ^b   Mansouri Torshizi, Hassan ^c   Ahmad, Faizan ^d  

^a KHARAZMI UNIVERSITY   (Iran)

^b UNIVERSITY OF TEHRAN   (Iran)

^c UNIVERSITY OF SISTAN AND BALUCHESTAN   (Iran)

^d JAMIA MILLIA ISLAMIA CENTRAL UNIVERSITY   (India)

Author keywords

Anticancer; Apoptosis; Pt(II) complex; Quenching; Casein

Indexed keywords

(BIPYRIDINE)(MORPHOLINE DITHIOCARBAMATE)PLATINUM(II); ANTINEOPLASTIC AGENT; CASEIN; PLATINUM COMPLEX;

APOPTOSIS; CHEMISTRY; CIRCULAR DICHROISM; DRUG EFFECTS; DRUG SCREENING; HUMAN; K-562 CELL LINE; METABOLISM; SPECTROFLUOROMETRY; SYNTHESIS; THERMODYNAMICS;

ANTINEOPLASTIC AGENTS; APOPTOSIS; CASEINS; CIRCULAR DICHROISM; DRUG SCREENING ASSAYS, ANTITUMOR; HUMANS; K562 CELLS; ORGANOPLATINUM COMPOUNDS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

EID: 84930090559     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-014-0364-z     Document Type: Article

References (45)

1. Semo, E., Kesselman, E., Danino, D., & Livney, Y. D. (2007). Casein micelle as a natural nano-capsular vehicle for nutraceuticals. Food Hydrocolloids,21, 936–942.
2. Zimet, P., Rosenberg, D., & Livney, Y. D. (2011). Re-assembled casein micelles and casein nanoparticles as nano-vehicles for ω-3 polyunsaturated fatty acids. Food Hydrocolloids,25, 1270–1276.
3. Elzoghby, A. O., El-Fotoh, W. S. A., & Elgindy, N. A. (2011). Casein-based formulations as promising controlled release drug delivery systems. Journal of Controlled Release,153, 206–216.
4. Caessens, P. W. J. R., Jongh, H. H. J. D., Norde, W., & Gruppen, H. (1999). The adsorption-induced secondary structure of β-casein and of distinct parts of its sequence in relation to foam and emulsion properties. Biochimica et Biophysica Acta,1430, 73–83.
5. Gaudin, J., Parc, A. L., Castrec, B., Ropersa, M., Choiseta, Y., Shchutskaya, J., et al. (2009). Engineering of caseins and modulation of their structures and interactions. Biotechnology Advances,27, 1124–1131.
6. Gangnard, S., Zuev, Y., Gaudin, J., Fedotov, V., Choiset, Y., Axelos, M. A. V., et al. (2007). Modifications of the charges at the N-terminus of bovine β-casein: Consequences on its structure and its micellisation. Food Hydrocolloids,21, 180–190.
7. Tompa, P. (2005). The interplay between structure and function in intrinsically unstructured proteins. FEBS Letters,579, 3346–3354. Budapest Spec Issue—Proteins and Peptides.
8. Farrell, H. M., Qi, P. X., & Uversky, V. N. (2006). New views of protein structure: applications to caseins. Advances in Biopolymers, A.C.S Symposium series,935, 52–70.
9. Yousefi, R., Gaudin, J., Chobert, J., Pourpak, Z., Moin, M., Moosavi-Movahedi, A. A., et al. (2009). Micellisation and immunoreactivities of dimeric β-caseins. Biochimica et Biophysica Acta,1794, 1775–1783.
10. Sawyer, L., & Holt, C. (1993). The secondary structure of milk proteins and their biological function. Journal of the Chemical Society, Faraday Transactions,89, 2683–2692.
11. Qi, P. X., Wickham, E. D., Piotrowski, E. G., Fagerquist, C. K., & Jr, H. M. F. (2005). Implication of C-terminal deletion on the structure and stability of bovine β-casein. The Protein Journal,24, 431–444.
12. Forrest, S. A., Yada, R. Y., & Rousseau, D. (2005). Interactions of vitamin D3 with bovine β-lactoglobulin A and β-casein. Journal of Agriculture and Food Chemistry,53, 8003–8009.
13. Lietaer, E., Poiffait, A., & Adrian, J. (1991). Interaction between casein and vitamin A. Lebens Wissen Technology,24, 39–45.
14. Shapira, A., Markman, G., Assaraf, Y. G., & Livney, Y. D. (2010). Beta-casein nanovehicles for oral delivery of chemotherapeutic drugs. Nanomedicine,6, 119–126.
15. Shapira, A., Assaraf, Y. G., & Livney, Y. D. (2010). β-casein-based nanovehicles for oral delivery of chemotherapeutic drugs: drug-protein interactions and mitoxantrone loading capacity. Nanomedicine,6, 547–555.
16. Liu, Y., & Guo, R. (2008). pH-dependent structures and properties of casein micelles. Biophysical Chemistry,136, 67–73.
17. Almeida, G. M., Duarte, T. L., Steward, W. P., & Jones, G. D. D. (2006). Detection of oxaliplatin-induced DNA crosslinks in vitro and in cancer patients using the alkaline comet assay. DNA Repair,5, 219–225.
18. Mansouri-Torshizi, H., I-Moghaddam, M., Divsalar, A., & Saboury, A. A. (2009). Diimine Platinum(II) and Palladium(II) complexes of dithiocarbamate derivative as potential antitumor agents: synthesis, characterization, cytotoxicity, and detail DNA-binding studies. Journal of Biomolecular Structure & Dynamics,26, 575–586.
19. Divsalar, A., Saboury, A. A., Mansoori-Torshizi, H., & Ahmad, F. (2010). Design, synthesis, and biological evaluation of a new Palladium(II) complex: Beta-lactoglobulin and K562 as targets. The Journal of Physical Chemistry B,114, 3639–3647.
20. Mansouri-Torshizi, H., Saeidifar, M., Khosravi, F., Divsalar, A., Saboury, A. A., & Yekke Ghasemi, Z. (2011). DNA-binding and thermodynamic parameters, structure and cytotoxicity of newly designed Platinum(II) and Palladium(II) anti-tumor complexes. Bulletin of the Korean Chemical Society,32, 947–955.
21. Divsalar, A., Saboury, A. A., Ahadi, L., Zemanatiyar, E., Mansouri-Torshizi, H., Ajloo, D., et al. (2011). Biological evaluation and interaction of a newly designed anti-cancer Pd(II) complex and human serum albumin. Journal of Biomolecular Structure and Dynamics,29(2), 283–296.
22. Marzano, C., Fregona, D., Baccichetti, F., Trevisan, A., Giovagnini, L., & Bordin, F. (2002). Cytotoxicity and DNA damage induced by a new Platinum(II) complex with pyridine and dithiocarbamate. Chemico-Biological Interactions,140, 215–229.
23. Mansouri-Torshizi, H., Srivastava, T. S., Perekh, H. K., & Chitnis, M. P. (1992). Synthesis, spectroscopic, cytotoxic, and DNA binding studies of binuclear 2,2′-bipyridine-platinum(II) and -palladium(II) complexes of meso-alpha, alpha’-diaminoadipic and meso-alpha, alpha’-diaminosuberic acids. Journal of Inorganic Biochemistry,45, 135–148.
24. Yang, J. T., Wu, C. S. C., & Martinez, H. M. (1981). Direct determination of absolute circular dichroism data and calibration of commercial instrument. Analytical Chemistry,53, 778.
25. Manavalan, P., & Johnson, C. J. R. (1987). Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Analytical Biochemistry,167, 76–85.
26. Divsalar, A., Saboury, A. A., Yousefi, R., Moosavi-Movahedi, A. A., & Mansoori-Torshizi, H. (2006). Spectroscopic and cytotoxic studies of the Novel designed Pd(II) complexes: beta-lactoglobulin and K562 as the targets. International Journal of Biological Macromolecules,40, 381–386.
27. Kubota, Y., Kubota, K., & Tani, S. (2000). DNA binding properties of DAPI (4′,6-diamidino-2-phenylindole) analogs having an imidazoline ring or a tetrahydropyrimidine ring: Groove-binding and intercalation. Nucleic Acids Symposium Series,44, 53–54.
28. Shpigelman, A., & Livney, Y. D. (2010). Thermally-induced protein polyphenol co-assemblies: beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG. Food Hydrocolloids,24, 735–743.
29. Geddes, C. D., & Lakowicz, J. R. (2005). Reviews in fluorescence (pp. 199–222). New York: Springer.
30. Atkinz, P., & Paula, J. (2006). Physical Chemistry (8th ed., p. 212). New York: Freeman, W.H. Company.
31. Zhang, Y., Qi, Z., Zheng, D., & Li, C. (2009). Interactions of Chromium (III) and Chromium (VI) with bovine serum albumin studied by UV spectroscopy, circular dichroism, and fluorimetry. Biological Trace Element Research,130, 172–184.
32. Cui, F., Zhang, Q., Yan, Y., Yao, X., Qu, G., & Lu, Y. (2008). Study of characterization and application on the binding between 5-iodouridine with HSA by spectroscopic and modeling. Carbohydrate Polymers,73, 464–472.
33. Lakowicz, J. R. (1999). In T. G. Dewey (Ed.), Principles of fluorescence spectroscopy (2nd ed.). New York: Plenum Press.
34. Liu, X. F., Xia, Y. M., & Fang, Y. J. (2005). Effect of metal ions on the interaction between bovine serum albumin and berberine chloride extracted from a traditional Chinese Herb coptis chinensis franch between. Journal of Inorganic Biochemistry,99, 1449–1457.
35. Timasheff, S. N. (1972). Thermodynamic of protein interactions. In H. Peeters (Ed.), Proteins of biological fluids. Oxford: Pergamon Press.
36. Rahman, M. H., Maruyama, T., Okada, T., Masaki, K. Y., & Otagiri, M. (1993). Study of interaction of carprofen and its enantiomers with human serum albumin-I mechanism of binding studied by dialysis and spectroscopic methods. Biochemical Pharmacology,46, 1721–1731.
37. Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions-forced contributing to stability. Biochemistry,20, 3096–3102.
38. Yamamoto, T., Yokoyama, M., Opanasopit, P., Hayama, A., Kawano, K., & Maitani, Y. (2007). What are determining factors for stable drug incorporation into polymeric micelle carriers? Consideration on physical and chemical characters of the micelle inner core. Journal of Controlled Release,123, 11–18.
39. Barzegar, A., Yousefi, R., Sharifzadeh, A., Dalgalarrondo, M., Chobert, J., Ganjali, M. R., et al. (2008). Chaperone activities of bovine and camel β-caseins: Importance of their surface hydrophobicity in protection against alcohol dehydrogenase aggregation. International Journal of Biological Macromolecules,42, 392–399.
40. Hendriks, J., Gensch, T., Hviid, L., van der Horst, M. A., Hellingwerf, K. J., & van Tho, J. J. (2002). transient exposure of hydrophobic surface in the photoactive yellow protein monitored with Nile Red. Biophysical Journal,82, 1632–1643.
41. Wallace, B. A., Lees, J. G., Orry, A. J. W., Lobley, A., & Janes, R. W. (2003). Analyses of circular dichroism spectra of membrane proteins. Protein Science,12, 875–884.
42. Farrell, H. M, Jr, Wickham, E. D., Unruh, J. J., Qi, P. X., & Hoagland, P. D. (2001). Secondry structural studies of bovine caseins: temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. Food Hydrocolloids,15, 341–354.
43. Hasni, I., Bourassa, P., Hamdani, S., Samson, G., Carpentier, R., & Tajmir-Riahi, H. A. (2011). Interaction of milk α- and β-caseins with tea polyphenols. Food Chemistry,126, 630–639.
44. Cui, F., Kong, X., Qin, L., Zhang, G., Liu, Q., Lei, B., et al. (2009). Specific interaction of 4-O-(a-l-Cladinosyl) daunorubicin with human serum albumin: The binding site II on HSA molecular using spectroscopy and modeling. Journal of Photochemistry and Photobiology B,95, 162–169.
45. Yue, Y., Chen, X., Qin, J., & Yao, X. (2009). Characterization of the mangiferin–human serum albumin complex by spectroscopic and molecular modeling approaches. Journal of Pharmaceutical and Biomedical Analysis,49, 753–759.