Effect of terahertz radiation on the transport properties of albumin: binding with metal ions

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Abstract

The effect of terahertz radiation on clusterization of bovine serum albumin (BSA) molecules and on BSA binding with nickel, cobalt and cadmium ions is investigated by means of high performance liquid chromatography and EPR spectroscopy under variation of the concentration of molecular oxygen in solution. Irradiation is detected to remove steric hindrance for oxygen adsorption. The degree of nickel and cobalt ion binding with irradiated BSA samples is substantially higher than with non-irradiated ones, while for cadmium the binding degree is the same and rather low in both cases. The functional groups in BSA molecule participating in metal ion binding are revealed by means of modeling.

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About the authors

E. F. Nemova

Institute of Laser Physics, Siberian Branch of the Russian Academy of Sciences

Author for correspondence.
Email: endy.endy@gmail.com
Russian Federation, Novosibirsk

T. V. Kobzeva

Voevodsky Institute of Chemical Kinetics and Combustion, Siberian Branch, Russian Academy of Sciences

Email: endy.endy@gmail.com
Russian Federation, Novosibirsk

G. G. Dultseva

Voevodsky Institute of Chemical Kinetics and Combustion, Siberian Branch, Russian Academy of Sciences

Email: endy.endy@gmail.com
Russian Federation, Novosibirsk

References

  1. Cherkasova O.P., Serdyukov D.S., Nemova E.F., Ratushnyak A.S., Kucheryavenko A.S., Dolganova I.N., Xu G., Skorobogatiy M., Reshetov I.V., Timashev P.S., Spektor I.E., Zaytsev K.I., Tuchin V.V. // J. Biomed. Optics, 2021. V. 26. P. 090902.
  2. Siegel P.H. // IEEE Trans. Microwave Theory Technol. 2004. V. 52. P. 2438−2447.
  3. Parrott E.P.J., Sun Y., Pickwell-MacPherson E. // J. Mol. Struct. 2011. 1006. P. 66−76.
  4. Cherkasova O.P., Fedorov V.I., Nemova E.F., Pogodin A.S. Optika I Spektroskopiya. 2009. V. 107. No. 4. P. 566. (In Russ.).
  5. Markelz A.G., Mittleman D.M. Photonics (ACS). https://doi.org/10.1021/acsphotonics.2c00228.
  6. Sitnikov D.S., Ilina I.V., Revkova V.A., Rodionov S.A., Gurova S.A., Shatalova R.O., Kovalev A.V., Ovchinnikov A.V., Chefonov O.V., Konoplyannikov M.A., Kalsin V.A., Baklaushev V.P. // Biomed. Opt. Express. 2021. No. 12. P. 7122.
  7. Yaekashiwa N, Yoshida H., Otsuki S, Hayashi S.I., Kawase K. // Photonics. 2019. No. 6. P. 33.
  8. Koyama S., Narita E., Suzuki Y., Shiina T., Taki M., Shinohara N., Miyakoshi J. // J. Radiat. Res. 2019. V. 60. P. 417.
  9. Shi W., Wang Y., Hou L., Ma C., Yang L., Dong C., Wang Z., Wang H., Guo J., Xu S., Li J. // J. Biophoton. 2021. V. 14. Article e202000237.
  10. Peng Y., Shi C., Wu X., Zhu Y., Zhuang S. // BME Frontiers. 2020. 2020. P. 1.
  11. Zaytsev K.I., Dolganova I.N., Chernomyrdin N.V., Katyba G.M., Gavdush A.A., Cherkasova O.P., Komandin G.A., Shchedrina M.A., Khodan A.N., Ponomarev D.S., Reshetov I.V., Karasik V.E., Skorobogatiy M., Kurlov V.N., Tuchin V.V. Journal of Optics. 2020. V. 22. No. 1. Article 013001. doi: 10.1088/2040-8986/ab4dc3.
  12. Son J.-H., Oh S.J., Cheon H.J. // Appl. Phys. 2019. V. 125. Article 190901.
  13. Wei L., Yu L., Jiaoqi H., Guorong H., Yang Z., Weiling F. // Frontiers in Laboratory Medicine. 2018. No. 2. P. 127.
  14. Di Fabrizio M., Lupi S., D’Arco A. // J. Phys.: Photonics. 2021. № 3. Article 032001.
  15. Schroer M.A., Schewa S., Gruzinov A. Y., Rönnau C., Lahey-Rudolph J.M., Blanchet C.E., Zickmantel T., Song Y.-H., Svergun D.I., Roessle M. // Sci. Rep. 2021. V. 11. P. 22311.
  16. Chen J.Y., Knab J.R., Ye S.J., He Y.F., Markelz A.G. // Appl. Phys. Lett. 2007. V. 90. 243901.
  17. Tan N.Y., Li R., Bräuer P., D’Agostino C., Gladden L.F., Zeitler J.A. // Phys. Chem. Chem. Phys. 2015. V. 17. P. 5999.
  18. Nemova E.F., Cherkasova O.P., Nikolaev N.A., Dultseva G.G. // Biophysics (Russian Federation). 2020. V. 65. No. 3. P. 410.
  19. Alhazmi H.A., Al Bratty M., Meraya A.M., Najmi A., Alam M.S., Javed S.A. // Acta Biochim. Pol. 2021. V. 68. No. 1. P. 99.
  20. Liu X.F., Xia Y.M., Fang Y. J. // Inorg Biochem. 2005. V. 99. No. 7. P. 1449. https://doi.org/10.1016/j.jinorgbio.2005.02.025. PMID: 15908003.
  21. Peng M., Shi S., Zhang Y. // Spectrochim Acta A Mol. Biomol. Spectrosc. 2012. V. 85. No. 1. P. 190. https://doi.org/10.1016/j.saa.2011.09.059.
  22. Hedberg Y.S., Dobryden I., Chaudhary H., Wei Z., Claesson P.M., Lendel C. // Colloids Surf B Biointerfaces. 2019. V. 173. P. 751.
  23. CRC Handbook of Chemistry and Physics. 95th edition. Ed. W.M. Haynes. CRC Press, 2014.

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2. Fig. 1. Scheme of the installation for irradiation of BSA film samples. To generate and detect THz radiation, pulses of the second harmonic of an erbium fiber laser are used (radiation wavelength - 775 nm, pulse duration - 130 fs, pulse repetition frequency - 77 MHz, average power - 80 mW). To convert laser radiation into THz radiation, a photoconductive antenna with gallium arsenide is used. The detection system consists of a 1 mm thick ZnTe (110) detector crystal, a quarter-wave plate, a Wollaston prism, photodiodes, an operational amplifier (OP-amp), and a lock-in detector.

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3. Fig. 2. Dependence of the integral intensity of the low-intensity triplet signal associated with BSA clusters on the oxygen content in the solution according to EPR spectroscopy data: circles—irradiated sample, squares—unirradiated.

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4. Fig. 3. Dependence of the content of BSA dimers (relative to their content in a non-irradiated solution with a maximum oxygen content) on the oxygen concentration in the solution according to high-performance liquid chromatography: circles - irradiated sample, squares - non-irradiated.

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