Optics and Spectroscopy

, Volume 110, Issue 4, pp 534–540

Optical, nanostructural, and biophysical properties of Zn-induced changes in human erythrocyte membranes

  • A. Ya. Khairullina
  • T. V. Ol’shanskaya
  • D. S. Filimonenko
  • N. M. Kozlova
  • Yu. M. Garmaza
  • E. I. Slobozhanina
Condensed-Matter Spectroscopy

DOI: 10.1134/S0030400X11040138

Cite this article as:
Khairullina, A.Y., Ol’shanskaya, T.V., Filimonenko, D.S. et al. Opt. Spectrosc. (2011) 110: 534. doi:10.1134/S0030400X11040138

Abstract

We studied changes in the surface of erythrocyte membranes exposed to the action of zinc sulfate in the concentration range of 0.1–2.0 mM/l using methods of light scattering, spectrofluorimetry, and atomic force microscopy. Using the spectrofluorimetry method, we revealed a dose-dependent increase in the fluorescence intensity of a fluorescamine probe incorporated into erythrocyte membranes modified by zinc ions, which is indicative of an increase in the level of NH2 groups on the cell surface. Using atomic force microscopy, we revealed changes in the surface topography of erythrocyte membranes exposed to the action of zinc sulfate in the concentration range of 0.1–2.0 mM/l. By performing a correlation analysis, we revealed that the correlation length of the autocorrelation function of the erythrocyte surface irregularity profile directly related to the fluorescence intensity of fluorescamine incorporated into erythrocyte membranes (r = 0.9, p < 0.05) modified by zinc ions. We showed that, in the zinc sulfate concentration range of 0.1–2.0 mM/l, zinc oxides form in erythrocyte membranes, which is confirmed by the appearance of an absorption band at 330–340 nm and by an increase in the light scattering. At more considerable concentrations, we identified absorption bands characteristic of zinc protein complexes in erythrocyte membranes. A considerable decrease in the elongation of the scattering indicatrix of erythrocyte membranes caused by luminescence correlates with the content of zinc proteins. Polarization measurements confirm the enhancement of the aggregation of protein complexes observed by the atomic force microscopy method. The proposed complex approach can be used in studies on the action of various abiotic factors on biological cells.

Copyright information

© Pleiades Publishing, Ltd. 2011

Authors and Affiliations

  • A. Ya. Khairullina
    • 1
  • T. V. Ol’shanskaya
    • 1
  • D. S. Filimonenko
    • 1
  • N. M. Kozlova
    • 2
  • Yu. M. Garmaza
    • 2
  • E. I. Slobozhanina
    • 2
  1. 1.B.I. Stepanov Institute of PhysicsNational Academy of Sciences of BelarusMinskBelarus
  2. 2.Institute of Biophysics and Cell EngineeringNational Academy of Sciences of BelarusMinskBelarus

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