Studies of Glutathione Reductase Inhibitors Activity of Copper(II) Complexes

Öz

(S)-(+) - phenylglycinol, (1S, 2R)-2-amino-1, 2-diphenylethanol and (R)-(+)-2-amino-1, 1, 3-triphenylpropanol based chiral copper (II) complex of Schiff bases were synthesized. The effects of these compounds on glutathione reductase enzyme were investigated. The best inhibitory effect was found to belong to complex 3.

Anahtar Kelimeler

• Schiff bases,copper (II) complexes,Glutathione Reductase

Bakır(II) Komplekslerinin Glutatyon Redüktaz İnhibitor Çalışması

Öz

(S)-(+)-fenilglisinol, (1S, 2R) -2-amino-1,2-difeniletanol’in ve (R)-(+)-2-amino-1,1,3-trifenilpropanol bazlı kiral Schiff bazlarının bakır (II) kompleksi sentezlendi. Bu bileşiklerin glutatyon redüktaz enzimi üzerindeki etkileri incelendi. En iyi inhibitör etkisinin kompleks 3'e ait olduğu belirlenmiştir.

Anahtar Kelimeler

• Schiff baz,bakır (II) kompleksleri,Glutatyon Redüktaz

Kaynakça

1. [1] Blanck, S., Maksimoska, J., Baumeister, J., Harms, K., Marmorstein, R., Meggers, E. (2012). “About the Art of Filling Protein Pockets Efficiently with Octahedral Metal Complexes”, Angew. Chem. Int. Ed. 51, 5244-5246.
2. [2] Barber, D., and Harris, S. (1994). “Oxygen free radicals and antioxidants: a review”. Journal of The American Pharmacists, NS34, 26-35.
3. [3] Yruela, I. (2005). “Copper in plants”, Brazilian Journal of Plant Physiology, 17, 145–156.
4. [4] Chena, H., Chena, J., Guona, Y., Wena, Y., Liub, J., Liub, W. (2012). “Evaluation of the role of the glutathione redox cycle in Cu(II) toxicity to green algae by a chiral perturbation approach”, Aquatic Toxicology, 120– 121, 19-26.
5. [5] Flikweet, J.P., Hoorn, R.K.J., Staal, G.E.J. (1974). “The effect of copper on human erythrocyte glutathione reductase”, Journal of Biochemistry, 649-653, 5.
6. [6] Rafter, G. W. (1982). “Copper inhibition of glutathione reductase and its reversal with gold thiolates, thiol, and disulfide compounds”, Biochemical Medicine, 27, 381-391.
7. [7] Vigouroux, S., Briand, M., and Briand, Y. (2004). “Linkage between the proteasome pathway and neurodegenerative diseases and aging”, Molecular Neurobiology, 30, 201-221.
8. [8] Willcox, J. K., Ash, S. L. and Catignani, G. L. (2004). “Antioxidants and prevention of chronic disease”, Critical Reviews in Food Science Nutrition, 44, 275-295.

9. [9] Meister, A., and Anderson, M. E. (1983). “Glutathione, Annual Reviev of.Biochemistry”, 52, 711-760. [10] Dolphin, D., Avramovic, O., and Poulson, R. (1989). “Coenzymes and Cofactors, III”, A, John Wiley & Sons, New York.
10. [11] Pullela, P., Chiku, T., Carvan, M., and Sem, D. S. (2006). “Fluorescence-based detection of thiols in vitro and in vivo using dithiol probes”, Analytical Biochemistry, 352, 265-273.
11. [12] Patsoukis, N. and Georgiou, C. (2004). “Determination of the thiol redox state of organisms: new oxidative stress indicators”, Analytical and Bioanalytical Chemistry, 378, 1783-1792.
12. [13] Asmis, R., Wang, Y., Xu, L., Kisgati, M., Begley, J. G., and Mieyal, J. J. (2005). “A novel thiol oxidation-based mechanism for adriamycin-induced cell injury in human macrophages”, The Journal of The Federation of American Societies for Experimental Biology, 19, 1866-1868.
13. [14] Patsoukis, N. and Georgiou, C. (2005). “Fluorometric determination of thiol redox state”, Analytical and Bioanalytical Chemistry, 383, 923-929.
14. [15] Henderson, B., Fairlamb, A. H., and Cerami, A. (1987). “Trypanothione dependent peroxide metabolism in Crithidia fasciculata and Trypanosoma brucei”, Molecular Biochemistry Parasitology, 24, 39-45.
15. [16] Fairlamb, A. H., Blackburn, P., Ulrich, P., Chait, B. T., and Cerami, A. (1985). “Trypanothione a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids”, Science, 222, 1485-1487. [17] Dolphin, D., Avramovic, O., and Poulson, R., (1989). “Glutathione reductase. In Glutathione: Chemical, Biochemical, and Medical Aspects. Part A”., Wiley-Interscience: New York, 553-596.
16. [18] Karplus, P. A., Krauth, S. R. L., Schirmer, R. H., and Schulz, G. E. (1988). “Inhibition of human glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-1- nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-1-nitrosourea. A crystallographic analysis”, European Journal Biochemistry, 171 (52), 193-198.
17. [19] Kumar, S., Dhar, D. N., Saxena, P. N. (2009). “Applications of metal complexes of Schiff bases-A review”, Journal of Scientific and Industrial Research, 68, 3, 181-187.
18. [20] Sadimenko, A. P. Edited by: Katritzky, A. R. (2012). “Organometallic Complexes of Pyridyl Schiff Bases”, Advances in Heterocyclic Chemistry, Book Series: Advances in Heterocyclic Chemistry, 107, 133-218.
19. [21] Katwal, R., Kaur, H., Kapur, B. K. (2013). “Applications of copper - Schiff's base complexes: a review”, Scientific Reviews & Chemical Communications, 3, 1, 1-15.
20. [22] Çolak, M., Aral, T., Hoşgören H., Demirel, N. (2007). Synthesis of Novel Chiral Schiff-Base Ligands and Their Application in Asymmetric Nitro Aldol (Henry) Reaction, Tetrahedron Asymmetry., 18, 1129.
21. [23] Tunç, T., Demirel, N., Emir, M., Günel, A., Çolak, M., Karacan, N. (2018). DNA binding and cleavage activity of three new copper (II) complexes of chiral N-salicyl-β-amino alcohol Schiff bases, J. Mex. Chem. Soc., 62(3), 51-66.
22. [24] Guan, X., Hoffman, B. N., McFarland, D. C., Gilkerson, K. K., Dwivedi, C., Erickson, A. K., Bebensee, S., and Pellegrini, J. (2002). Glutathione and mercapturic acid conjugates of sulofenur and their activity against a human colon cancer cell line, Drug Metabolism and Disposition, 30, 331-335.
23. [25] Rafter, W. G. (1981). Copper inhibition of glutathione reductase and its reversal with gold thiolates, thiol, and disulfide compounds, Biochemical Medicine, 27, 381-391.