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Investigation of molecular mechanisms of action of chelating drugs on protein-lipid model membranes by X-ray fluorescence

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Abstract

Protein-lipid films based on the enzyme alkaline phosphatase were subjected to the action of chelating drugs, which are used for accelerating the removal of heavy metals from the human body, and the elemental composition of the resulting films was investigated. Total-reflection X-ray fluorescence measurements were performed at the Berlin Electron Storage Ring Company for Synchrotron Radiation (BESSY) in Germany. A comparative estimation of the protective effect of four drugs (EDTA, succimer, xydiphone, and mediphon) on membrane-bound enzymes damaged by lead ions was made. The changes in the elemental composition of the protein-lipid films caused by high doses of chelating drugs were investigated. It was shown that state-of-the-art X-ray techniques can, in principle, be used to develop new methods for the in vitro evaluation of the efficiency of drugs, providing differential data on their actions.

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Authors and Affiliations

  1. Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskiĭ pr. 59, Moscow, 119333, Russia

    S. I. Zheludeva, M. V. Koval’chuk & N. D. Stepina

  2. Russian Research Center, Kurchatov Institute, pl. Kurchatova, Moscow, 123182, Russia

    N. N. Novikova

  3. Berlin Electron Storage Ring Company for Synchrotron Radiation, Albert-Einstein Straé 15, D-12489, Berlin, Germany

    A. I. Erko

  4. Moscow Research Institute of Pediatrics and Pediatric Surgery, Ministry of Health of the Russian Federation, Taldomskaya ul. 2, Moscow, 125412, Russia

    E. A. Yur’eva

Authors
  1. N. N. Novikova
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  2. S. I. Zheludeva
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  3. M. V. Koval’chuk
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  4. N. D. Stepina
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  5. A. I. Erko
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  6. E. A. Yur’eva
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Corresponding author

Correspondence to N. N. Novikova.

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Novikova, N.N., Zheludeva, S.I., Koval’chuk, M.V. et al. Investigation of molecular mechanisms of action of chelating drugs on protein-lipid model membranes by X-ray fluorescence. Crystallogr. Rep. 54, 1208–1213 (2009). https://doi.org/10.1134/S1063774509070128

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  • DOI: https://doi.org/10.1134/S1063774509070128

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