Thermodynamic Aspects of Binding Proteins with Porphyrins. Spectral and Thermochemical Approaches

Natalya Sh. Lebedeva,^a Yury A. Gubarev,^a Alexey V. Lyubimtsev,^b Elena S. Yurina,^a and Oskar I. Koifman^b

^aG.A. Krestov Institute of Solution Chemistry of Russian Academy of Sciences, 153045 Ivanovo, Russia

^bResearch Institute of Macroheterocycles, Ivanovo State University of Chemistry and Technology, 153000 Ivanovo, Russia

DOI: 10.6060/mhc160530g

Macroheterocycles 2017 10(1) 37-42

The results of spectral and thermochemical studies of the interaction of bovine serum albumin with anionic and cationic porphyrins are presented in this paper. The limits of different methods for the determination of binding constants and thermodynamic parameters were shown. On the basis of spectral studies the binding constants of albumin with the porphyrins were evaluated. The fluorescence quenching constants of the protein at the porphyrins titration were estimated and it was found that in the albumin-porphyrin systems the static and dynamic quenching mechanisms are combined. The thermodynamic parameters were determined using of Van’t Hoff equation from spectral data and the method of isothermal titration calorimetry. It was established that the stability constant of anionic complex is higher than that for complex of cationic porphyrin with albumin.

References:

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1. Zhang W., Zhang L., Ping G., Zhang Y., Kettrup A. J. Chromatogr. B 2002, 768, 211-214.
https://doi.org/10.1016/S0378-4347(01)00501-1

2. Hou A.-X., Qu S.-S., Wong W.-K., Liu Y. Acta Physicochimica Sinica 2003, 19, 134-138.
https://doi.org/10.3866/PKU.WHXB20030209

3. Sehlstedt U., Kim S.K., Carter P., Goodisman J., Vollano J.F., Norden B., Dabrowiak J.C. Biochemistry 1994, 33, 417-426.
https://doi.org/10.1021/bi00168a005

4. Dougherty T.J., Gomer C.J., Henderson B.W., Jori G., Kessel D., Korbelik M., Moan J., Peng Q. J. Natl. Cancer Inst. 1998, 90, 889-905.
https://doi.org/10.1093/jnci/90.12.889

5. Brown S.B., Shillcock M., Jones P. Biochem. J 1976, 153, 279-285.
https://doi.org/10.1042/bj1530279

6. Kano K., Fukuda K., Wakami H., Nishiyabu R., Pasternack R.F. J. Am. Chem. Soc. 2000, 122, 7494-7502.
https://doi.org/10.1021/ja000738g

7. Daly D., Al-Sabi A., Kinsella G., Nolan K., Dolly J. Chem. Commun. 2015, 51, 1066-1069.
https://doi.org/10.1039/C4CC05639F

8. Gomes M.C., Silva S., Faustino M.A., Neves M.G., Almeida A., Cavaleiro J.A., Tomé J.P., Cunha Â. Photochemical & Photobiological Sciences 2013, 12, 262-271.
https://doi.org/10.1039/C2PP25149C

9. Beynon R., Easterby J. Buffer Solutions: the Basics, Oxford: Oxford University Press, 1996. 88 p.

10. Guo M., Zou J.-W., Yi P.-G., Shang Z.-C., Hu G.-X., Yu Q.-S. Anal. Sci. 2004, 20, 465-470.
https://doi.org/10.2116/analsci.20.465

11. An W., Jiao Y., Dong C., Yang C., Inoue Y., Shuang S. Dyes and Pigments 2009, 81, 1-9.
https://doi.org/10.1016/j.dyepig.2008.08.004

12. Lu S., Yu X., Yang Y., Li X. Spectrochim. Acta, Pt. A: Mol. Biomol. Spectrosc. 2012, 99, 116-121.

http://dx.doi.org/10.1016/j.saa.2012.09.012

13. Lebedeva N.S., Mikhailovskii K., V'yugin A. Russ. J. Phys. Chem. 2001, 75, 1031-1033.

14. Lebedeva N.S., Pavlycheva N., V'yugin A. Russ. J. Phys. Chem. 2003, 77, 364-367.

15. Borissevitch I.E., Tominaga T.T., Imasato H., Tabak M. J. Lumin. 1996, 69, 65-76.
https://doi.org/10.1016/0022-2313(96)00037-3

16. Li Y., Jia B., Wang H., Li N., Chen G., Lin Y., Gao W. Colloids Surf. B. Biointerfaces 2013, 104, 311-317.
https://doi.org/10.1016/j.colsurfb.2012.12.023

17. Cantor C.R., Schimmel P. Journal of Solid-Phase Biochemistry 1980, 5(3).

18. Kubát P., Lang K., Mosinger J., Wagnerová D. Z. Phys. Chem. 1999, 210, 243-256.

19. Lang K., Mosinger J., Wagnerová D. Coord. Chem. Rev. 2004, 248, 321-350.
https://doi.org/10.1016/j.ccr.2004.02.004

20. Roswell L.B. Protein Conformation: New Research, New York: Nova Publishers, 2008.

21. Chang R. Physical chemistry with applications to biological systems; New York: Collier Macmillan Ltd, 1977.

22. Zhao P., Huang J.-W., Ji L.-N. Spectrochim. Acta, Pt. A: Mol. Biomol. Spectrosc. 2012, 88, 130-136.

http://dx.doi.org/10.1016/j.saa.2011.12.017

23. Yu X., Liu R., Yi R., Yang F., Huang H., Chen J., Ji D., Yang Y., Li X., Yi P. Spectrochim. Acta, Pt. A: Mol. Biomol. Spectrosc. 2011, 78, 1329-1335.

http://dx.doi.org/10.1016/j.saa.2011.01.024

24. Durmuş M., Yaman H., Göl C., Ahsen V., Nyokong T. Dyes and Pigments 2011, 91, 153-163.
https://doi.org/10.1016/j.dyepig.2011.02.007

25. Sibirtsev V., Garabadzhiu A., Ivanov S. Russ. J. Bioorg. Chem. 2001, 27, 57-65.
https://doi.org/10.1023/A:1009535320077

26. Bobrovnik S. Ukrainian Biochemistry Journal 2004, 76, 5-28 (in Ukr.).

27. Monkos K. General physiology and biophysics 2013, 32, 67-78.
https://doi.org/10.4149/gpb_2013011

28. Lebedeva N., Malkova E., Syrbu S., Gubarev Y., Nikitin D. Int. J. Biochem. Biophys. 2014, 2, 13-18.
https://doi.org/10.13189/ijbb.2014.020103

29. Hill N. Journal of Physics C: Solid State Physics 1970, 3, 238.
https://doi.org/10.1088/0022-3719/3/1/026

30. Sudlow G., Birkett D.J., Wade D.N. Clin. Exp. Pharmacol. Physiol. 1975, 2, 129-140.
https://doi.org/10.1111/j.1440-1681.1975.tb01826.x

31. Fanali G., di Masi A., Trezza V., Marino M., Fasano M., Ascenzi P. Molecular aspects of medicine 2012, 33, 209-290.
https://doi.org/10.1016/j.mam.2011.12.002

32. Sugio S., Kashima A., Mochizuki S., Noda M., Kobayashi K. Protein Eng. 1999, 12, 439-446.
https://doi.org/10.1093/protein/12.6.439

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Thermodynamic Aspects of Binding Proteins with Porphyrins. Spectral and Thermochemical Approaches

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