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SPECTROSCOPIC STUDY OF THE BINDING OF NETROPSIN AND HOECHST 33258 WITH NUCLEIC ACIDS

Abstract

The interaction of the groove binding compounds - peptide antibiotic netropsin and fluorescent dye (bis-benzimidazole) Hoechst 33258 - with the double-stranded DNA and synthetic double-stranded polynucleotide poly(rA)-poly(rU) has been studied by spectrophotometry. The absorption spectra of these ligand complexes with the nucleic acids have been obtained. Spectral changes at the complexation of individual ligands with the mentioned nucleic acids reveal the similarity of binding of each of these ligands with both DNA and RNA. Based on the spectroscopic measurements, the parameters of netropsin and Hoechst 33258 binding with DNA and poly(rA)-poly(rU) - K and n, as well as the thermodynamic parameters DS, DG, and DH have been determined. It is found that the binding of Hoechst 33258 with both nucleic acids is accompanied by a positive change in enthalpy, while in the case of netropsin the change in enthalpy is negative. Moreover, the contribution of the entropy factor to the formation of the complexes is more pronounced in the case of Hoechst 33258.

About the Authors

P. O. Vardevanyan
Yerevan State University
Russian Federation


M. A. Parsadanyan
Yerevan State University
Russian Federation


A. P. Antonyan
Yerevan State University
Russian Federation


V. G. Sahakyan
Yerevan State University
Russian Federation


References

1. D. Rentzeperis, L. A. Marky, T. J. Dwyer, B. H. Gelerstanger, J. G. Pelton, D. E. Wemmer. Biochemistry, 34, N 9 (1995) 2937-2945

2. A. N. Lane, T. C. Jenkins. Q. Rev. Biophys., 33, N 3 (2000) 255-306

3. S. K. R. Gowda, B. B. Mathew, C. N. Sudhmani, H. S. B. Naik. Biomed. Biotechnol., 2, N 1 (2014) 1-6

4. T. H. Doung, K. Zakrzewska. J. Biomol. Struct. Dyn., 14, N 6 (1997) 691-701

5. Y.-Y. Fang, V. R. Morris, G. M. Lingani, W. M. Southerland. Open Conf. Proc. J., N 1 (2010) 157-163

6. Ю. С. Бабаян, Л. Е. Ксодо, Дж. Манзини. Биофизика, 33, N 4 (1988) 716-721

7. E. A. Lewis, M. Munde, S. Wang, M. Retting, V. Le, V. Machha, W. D. Wilson. Nucl. Аcid. Res., 39, N 22 (2011) 9649-9658

8. В. Зенгер. Принципы структурной организации нуклеиновых кислот, Москва, Мир (1987) 418-520

9. R. Palchaudhuri, P. J. Hergenrother. Curr. Opt. Biotechnol., 18, N 6 (2007) 497-503

10. K. Mišković, M. Bujak, M. B. Loncar, L. Glavas-Obrovac. Arh. Hig. Rad. Toxicol., 64, N 4 (2013) 593-602

11. T. Yamori, A. Matsunaga, S. Sato, K. Yamazaki, A. Komi, K. Ishizu, I. Mita, H. Edatsugi. Cancer Res., 59 (1999) 4042-4049

12. M. H. David-Cordonnier, M. P. Hildebrand, B. Baldeyrou, A. Lansiaux, C. Keuser. Eur. J. Med. Chem., 42 (2007) 752771

13. B. K. Bhuyan, K. A. Newell, S. L. Crampton, D. D. Von Hoff. Cancer Res., 42 (1982) 3532-3537

14. X. Wanga, N. Chub, N. Wanga, L. Q. Chao, C. Jianga, X. Wanga, T. Ikejima, M. Chenga. Bioorg. Med. Chem. Lett., 22 (2012) 6297-6300

15. M. Hirota, T. Fujiwara, S. Mineshita, H. Sugiyama, H. Teraoka. Int. J. Biochem. Cell. Biol., 39 (2007) 988-996

16. В. В. Костюков, М. П. Евстигнеев. Физика живого, 18, N 2, (2010) 34-40

17. B. Nguen, S. Neidle, D. W. Wilson. Acc. Chem. Res., 42 (2009) 11-21

18. N. N. Degtyareva, B. D. Wallace, A. R. Bryant, K. M. Loo, J. T. Petty. Biophys. J., 92 (2007) 959-965

19. X. Shi, R. B. J. Macgregor. Biophys. Chem., 125 (2007) 471-482

20. П. О. Вардеванян, М. А. Парсаданян, А. П. Антонян, С. Н. Акопян. Журн. физ. химии, 91, N 6 (2017) 1071-1073

21. D. R. Corey. J. Clin. Invest., 117 (2007) 3615

22. C. N. N’soukpoe-Kossi, C. Descoteaux, E. Asselin, H. A. Tajmir-Riahi, G. Berube. DNA Cell Biol., 27 (2008) 1

23. S. R. Kirk, Y. Tor. Bioorg. Med. Chem., 7 (1999) 1979

24. S. Fulle, H. Gohlke. J. Mol. Recognit., 23 (2010) 220

25. S. Nafisi, F. Manouchehri, M. Bonsaii. J. Photochem. Photobiol. B: Biol., 111 (2012) 27

26. D. Khaitan, M. E. Dinger, J. Mazar, J. Crawford, M. A. Smith, J. S. Mattick, R. J. Perera. Cancer Res., 71 (2011) 3852

27. Д. Фрайфельдер. Физическая биохимия, Москва, Мир (1980)

28. J. Lah, N. Carl, I. Drobnak, B. Šumiga, G. Vesnaver. Acta Chim. Slov., 53 (2006) 284

29. S. Y. Breusegem, F. G. Loontiens, P. Regenfuss, R. M. Clegg. Methods Enzyme J., 340 (2001) 212

30. I. H. Stockley. In “Stockley’s Drug Interactions”, 6th ed., London, Pharm. Press (2002) 1080-1081

31. L. Tabernero, N. Verdaguer, M. Coll, I. Fita, G. A. van der Marel, J. H. van Boom, A. Rich, J. Aymami. Biochemistry, 32, N 33 (1993) 8403-8410

32. P. O. Vardevanyan, A. P. Antonyan, M. A. Parsadanyan, K. V. Pirumyan, A. M. Muradyan, A. T. Karapetian. J. Biomol. Struct. Dyn., 25, N 6 (2008) 641-646

33. J. A. Parkinson, S. E. Ebrahimi, J. H. Mckie, K. T. Douglas. J. Biochem., 33 (1994) 8442-8452


Review

For citations:


Vardevanyan P.O., Parsadanyan M.A., Antonyan A.P., Sahakyan V.G. SPECTROSCOPIC STUDY OF THE BINDING OF NETROPSIN AND HOECHST 33258 WITH NUCLEIC ACIDS. Zhurnal Prikladnoii Spektroskopii. 2018;85(2):321-326. (In Russ.)

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