Abstract
The interaction of nutritional preservative and dye erythrosine B with bovine serum albumin (BSA) under the influence of millimeter range electromagnetic waves (MM EMW) with frequencies 41.8 and 51.8 GHz has been studied by the UV-denaturation and spectroscopic methods (absorption, fluorescence, and circular dichroism (CD)). We show that the irradiation by MM EMW with the frequency 51.8 GHz stabilizes the complex BSA-erythrosine B. At the same time, denaturation parameters of the complex at the irradiation of BSA solution with the frequency 41.8 GHz do not differ from those obtained for non-irradiated samples within the limits of experimental error. We also show that under the influence of the irradiation by 51.8 GHz frequency there is no conformational change of BSA. However, a change in the protein conformation takes place in the case of the complex BSA-erythrosine B. In addition, the complex-formation process is thermodynamically beneficial and implemented because of the additional hydrogen bonds and van-der-Waals interaction between BSA and erythrosine B under the influence of MM EMW.
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This work was supported by ongoing institutional funding. No additional grants to carry out or direct this particular research were obtained.
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Translated by V. Musakhanyan
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Parsadanyan, M.A., Shahinyan, M.A., Grigoryan, S.V. et al. Interaction of Serum Albumin with Erythrosine B under the Influence of Millimeter-Range Electromagnetic Waves. J. Contemp. Phys. 58, 428–434 (2023). https://doi.org/10.1134/S106833722304014X
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DOI: https://doi.org/10.1134/S106833722304014X