Competition between two quinacrine–dna binding modes from polarized fluorescence data
Abstract
Binding of acridine derivative quinacrine (QA) to chicken erythrocyte DNA was studied by methods of
absorption and polarized fluorescent spectroscopy. Measurements were carried out in aqueous buffered
solutions (pH 6.9) of different dye concentrations ([QA] = 10-6÷ 10-4 M) and ionic strengths ([Na+] = 10-3÷ 0.15 M) in a wide range of phosphate-to-dye molar ratios (P/D). It is established that the minimum of fluorescent titration curve plotted as relative fluorescence intensity vs P/D is conditioned by the competition between the two types of QA binding to DNA which posses by different emission parameters: (i) intercalative one dominating under high P/D values, and (ii) outside electrostatic binding dominating under low P/D values, which is accompanied by the formation of non-fluorescent dye associates on the DNA backbone. Absorption and fluorescent characteristics of complexes formed were determined. The method of calculation of different binding modes contribution to the complex formation depending on P/D value is presented. It was shown that the size of binding site measured as the number of DNA base pairs per one QA molecule bound in the case of the electrostatic interaction is 8 times less than that for the intercalative one, that determines the competitive ability of the outside binding against the stronger intercalative binding mode.
Downloads
References
2. DNA binding fluorochromes for the study of the organization of the metaphase nucleus / T. Caspersson, L. Zech, E.J. Modest, [et al.] // Exp. Cell Res. – 1969. –V. 58(1). – P. 141-152.
3. Chemical differentiation along metaphase chromosomes / T. Caspersson, L. Zech, C. Johansson, E.L. Modest // Chromosoma. – 1970. – V. 30(2). – P. 215–227.
4. Goodman L.S. The Pharmacological Basis of Therapeutics. 5th ed. / L.S. Goodman, A. Gilman. - New York: Macmillan, 1975. – P. 1030–1032.
5. Wallace D.J. The use of quinacrine (Atabrine) in rheumatic diseases: a reexamination / D.J. Wallace // Semin. Arthritis Rheum. – 1989. – V. 18. – P. 282–297.
6. Treatment of transmissible spongiform encephalopathy by intraventricular drug infusion in animal models / K. Doh-ura, K. Ishikawa, I. Murakami-Kubo, [et al.] // J. Virol. – 2004. – V. 78. – V. 4999–5006.
7. Ferguson L.R. Genotoxicity of non-covalent interactions: DNA intercalators / L.R. Ferguson, W.A. Denny // Mutat. Res. – 2007. – V. 623(1-2). – P. 14-23.
8. Krzyminski K. Spectral properties of substituted 9-(phenoxycarbonyl)-acridines and related cations: experimental and theoretical investigations / K. Krzyminski, A.D. Roshal, A. Niziolek // Spectrochim. Acta A Mol. Biomol. Spectrosc. – 2008. – V. 70(2). – P. 394–402.
9. Valencia C. Quantum yields of singlet molecular oxygen , O2(1Δg), produced by antimalaric drugs in organic solvents / C. Valencia, E. Lemp, A.L. Zanocco // J. Chil. Chem. Soc. – 2003. – V. 48(4). – P. 17–21.
10. DNA-damaging activity and mutagenicity of 16 newly synthesized thiazolo[5,4-a]acridine derivatives with high photo-inducible cytotoxicity / C. Di Giorgio, A. Nikoyan, L. Decome, [et al.] // Mutat Res. – 2008. – V. 650(2). – P. 104-114.
11. Porumb H. The solution spectroscopy of dtugs and the drug – nucleic acid interactions / H. Porumb // Progr. Biophys. Mol. Biol. – 1978. – V. 37. – P. 175–195.
12. Berman H.M. The interaction of intercalating drugs with nucleic acids / H.M. Berman, P.R. Young // Annu. Rev. Biophys. Bioeng. – 1981. – V. 10. – P. 87–114.
13. Li H.J. Relaxation studies of the proflavine-DNA complex: the kinetics of an intercalation reaction / H.J. Li, D.M. Crothers // J. Mol. Biol. – 1969. – V. 39. – P. 461-477.
14. Schmechle D.E.V. Kinetic and hydrodynamic studies of the complex of proflavine with polyA∙polyU / D.E.V. Schmechle, D.M. Crothers // Biopolymers. – 1971. – V. 10(3). – P. 465-480.
15. Nakamoto K. Drug-DNA interactions: structures and spectra. V. 51 / K. Nakamoto, M. Tsuboi, G.D. Strahan - John Wiley & Sons, 2008. - 370 p.
16. Wilson W.D. Analysis of cooperativity and ion effects in the interaction of quinacrine with DNA / W.D. Wilson, J.G. Lopp // Biopolymers. – 1979. – V. 18(12). – P. 3025–3041.
17. Говор И.Н. Стабилизатор мощности излучения ОКГ / И.Н. Говор, В.М. Нестеренко // Приборы и техника эксперимента. – 1974. – № 3. – C. 168–169.
18. Fluorescence and binding properties of phenazine derivatives in complexes with polynucleotides of various base composition and secondary structure / V. Zozulya, Yu. Blagoi, G. Lober, I. Voloshin, [et al.] // Biophys. Chem. –1997 – V. 65. - P. 55-63.
19. Lakowicz J.R. Principles of Fluorescent Spectroscopy 2nd ed. / J.R. Lakowicz - Kluwer Academic/Plenum Press, New York, 1999. – 362 p.
20. Schwarz G. Thermodynamic and kinetic studies on the cooperative binding of proflavine to linear polyanions / G. Schwarz, S. Klose // Eur. J. Biochem. – 1972. – V. 29. – P. 249-256.
21. Interaction of phenosafranine with nucleic acids and model polyphosphates. I. Self-aggregation and complex formation with inorganic polyphosphates / Z. Balcarova, V. Kleinwachter; J. Koudelka, [et al.] // Biophys. Chemistry. – 1978. – V. 8. – P. 17–25.
22. Zozulya V.N. Cooperative binding of daunomycin and carminomycin to inorganic polyphosphate / V.N. Zozulya, V.F. Fyodorov, Yu.P. Blagoi // Studia Biophysica. – 1990. – V. 137 (1-2). – P. 17–28.
23. Pachman U. Quantum yield of acridines interacting with DNA of defined base sequence. A basis for the explanation of acridine bands in chromosomes / U. Pachman, R. Rigler // Exper. Cell. Res. – 1972. – V. 72(2). – P. 602–608.
24. Borisova O.F. Evidence for quinacrine fluorescence on three AT pairs of DNA / O.F. Borisova, A.P. Razjivin, V.I. Zaregogorodsev // FEBS Letters. – 1974. – V. 46. – P. 239–242.
25. Fluorescence analysis of GC versus AT binding of quinacrine to DNA / G. Baldini, S. Doglia, G. Sassi, G. Lucchini // Int. J. Biol. Macromol. – 1981. – V. 3. – P. 248–252.
26. Studies of cationic and neutral form of acridine compound interaction with nucleic acids / G.G. Sheina, A.P. Limansky, T.F. Stepanova, Yu.P. Blagoi // Stud. biophys. – 1984. – V. 100(3). – P. 187–194.
27. Zozulya V.N. Cooperative binding of quinacrine to inorganic polyphosphate / V.N. Zozulya, I.M. Voloshin // Biophysical chemistry. – 1994. – V. 48. – P. 353–358.
28. Deranleau D.A. Estimation of the saturation fraction of bound fluorescent ligands from intensity and anisotropy of the emission / D.A. Deranleau, Th. Binkert, P. Bally // J. Theor. Biol. – 1980. – V. 86. – P. 477–485.
29. Weber G. Polarization of the fluorescence of macromolecules. 1. Theory and experimental method / G. Weber // Biochem. J. – 1952. – V. 51. – P. 145–155.
30. McGhee J.D. Theoretical aspects of DNA-Protein interactions: Cooperative and noncooperative binding of large ligands to a one-dimensional homogeneous lattice / J.D. McGhee, P.H. Von Hippel // J. Mol. Biol. – 1974. – V. 86. – P. 469–489.
31. Aslanoglu M. Voltammetric studies of the interaction of quinacrine with DNA / M. Aslanoglu, G. Ayne // Anal. Bioanal. Chem. – 2004. – V. 380(4). – P. 658–663.
32. DNA bifunctional intercalators. 2. Fluorescence properties and DNA binding interaction of an ethidium homodimer and acridine ethidium heterodimer / B. Gaugain, J. Barbert, N. Capelle, [et al.] // Biochemistry. – 1978. – V.17 (24). – P. 5078–5088.
Authors who publish with this journal agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
- Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.
- Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).