The interaction of groove binding compounds — peptide antibiotic (polyamide) netropsin and fluorescent dye (bisbenzimidazole) Hoechst 33258 — with the double-stranded DNA and synthetic double-stranded polynucleotide poly(rA)-poly(rU) has been studied by spectrophotometry. Absorption spectra of these ligand complexes with 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 binding parameters of netropsin and Hoechst 33258 binding to DNA and poly(rA)-poly(rU) – K and n, as well as the thermodynamic parameters ΔS, ΔG, and ΔH have been determined. It was found that the binding of Hoechst 33258 to 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 entropy to the formation of the complexes is more pronounced in the case of Hoechst 33258.
Similar content being viewed by others
References
D. Rentzeperis, L. A. Marky, T. J. Dwyer, B. H. Gelerstanger, J. G. Pelton, and D. E. Wemmer, Biochemistry-US, 34, No. 9, 2937–2945 (1995).
A. N. Lane and T. C. Jenkins, Q. Rev. Biophys., 33, No. 3, 255–306 (2000).
S. K. R. Gowda, B. B. Mathew, C. N. Sudhmani, and H. S. B. Naik, Biomed. Biotechnol., 2, No. 1, 1–6 (2014).
T. H. Doung and K. Zakrzewska, J. Biomol. Struct. Dyn., 14, No. 6, 691–701 (1997).
Y.-Y. Fang, V. R. Morris, G. M. Lingani, and W. M. Southerland, Open Conf. Proc. J., No. 1, 157–163 (2010).
Yu. S. Babayan, L. E. Xodo, and G. Manzini, Biophysics [in Russian], 33, No. 4, 716–721 (1988).
E. A. Lewis, M. Munde, S. Wang, M. Retting, V. Le, V. Machha, and W. D. Wilson, Nucl. Аcid. Res., 39, No. 22, 9649–9658 (2011).
V. Zenger, Principles of the Structural Organization of Nucleic Acids [in Russian], Mir, Moscow, 418–520 (1987).
R. Palchaudhuri and P. J. Hergenrother, Curr. Opt. Biotechnol., 18, No. 6, 497–503 (2007).
K. Mišković, M. Bujak, M. B. Loncar, and L. Glavas-Obrovac, Arh. Hig. Rad. Toxicol., 64, No. 4, 593–602 (2013).
T. Yamori, A. Matsunaga, S. Sato, K. Yamazaki, A. Komi, K. Ishizu, I. Mita, and H. Edatsugi, Cancer Res., 59, 4042–4049 (1999).
M. H. David-Cordonnier, M. P. Hildebrand, B. Baldeyrou, A. Lansiaux, and C. Keuser, Eur. J. Med. Chem., 42, 752771 (2007).
B. K. Bhuyan, K. A. Newell, S. L. Crampton, and D. D. Von Hoff, Cancer Res., 42, 3532–3537 (1982).
X. Wanga, N. Chub, N. Wanga, L. Q. Chao, C. Jianga, X. Wanga, T. Ikejima, and M. Chenga, Bioorg. Med. Chem. Lett., 22, 6297–6300 (2012).
M. Hirota, T. Fujiwara, S. Mineshita, H. Sugiyama, and H. Teraoka, Int. J. Biochem. Cell. Biol., 39, 988–996 (2007).
V. V. Kostyukov and M. P. Evstigneev, The Physics of the Living [in Russian], 18, No. 2, 34–40 (2010).
B. Nguen, S. Neidle, and D. W. Wilson, Acc. Chem. Res., 42, 11–21 (2009).
N. N. Degtyareva, B. D. Wallace, A. R. Bryant, K. M. Loo, and J. T. Petty, Biophys. J., 92, 959–965 (2007)
X. Shi and R. B. J. Macgregor, Biophys. Chem., 125, 471–482 (2007)
P. O. Vardevanyan, M. A. Parsadanyan, A. P. Antonyan, and S. N. Akopyan, Zh. Fiz Khim., 91, No. 6, 1071–1073 (2017).
D. R. Corey, J. Clin. Invest., 117, 3615 (2007).
C. N. N'soukpoe-Kossi, C. Descoteaux, E. Asselin, H. A. Tajmir-Riahi, and G. Berube, DNA Cell Biol., 27, 1 (2008).
S. R. Kirk and Y. Tor, Bioorg. Med. Chem., 7, 1979 (1999).
S. Fulle and H. Gohlke, J. Mol. Recognit., 23, 220 (2010).
S. Nafisi, F. Manouchehri, and M. Bonsaii, J. Photochem. Photobiol. B: Biol., 111, 27 (2012).
D. Khaitan, M. E. Dinger, J. Mazar, J. Crawford, M. A. Smith, J. S. Mattick, and R. J. Perera, Cancer Res., 71, 3852 (2011).
D. Freifelder, Physical Biochemistry [in Russian], Mir, Moscow (1980)
J. Lah, N. Carl, I. Drobnak, B. Šumiga, and G. Vesnaver, Acta Chim. Slov., 53, 284 (2006).
S. Y. Breusegem, F. G. Loontiens, P. Regenfuss, and R. M. Clegg, Methods Enzyme J., 340, 212 (2001).
I. H. Stockley, In: Stockley′s Drug Interactions, 6th edn., Pharm. Press, London (2002), pp. 1080–1081.
L. Tabernero, N. Verdaguer, M. Coll, I. Fita, G. A. van der Marel, J. H. van Boom, A. Rich, and J. Aymami, Biochemistry, 32, No. 33, 8403–8410 (1993).
P. O. Vardevanyan, A. P. Antonyan, M. A. Parsadanyan, K. V. Pirumyan, A. M. Muradyan, and A. T. Karapetian, J. Biomol. Struct. Dyn., 25, No. 6, 641–646 (2008).
J. A. Parkinson, S. E. Ebrahimi, J. H. Mckie, and K. T. Douglas, J. Biochem., 33, 8442–8452 (1994).
Author information
Authors and Affiliations
Corresponding author
Additional information
Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 85, No. 2, pp. 321–326, March–April, 2018.
Rights and permissions
About this article
Cite this article
Vardevanyan, P.O., Parsadanyan, M.A., Antonyan, A.P. et al. Spectroscopic Study of the Binding of Netropsin and Hoechst 33258 to Nucleic Acids. J Appl Spectrosc 85, 335–340 (2018). https://doi.org/10.1007/s10812-018-0653-1
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s10812-018-0653-1