Interaction of Serum Albumin with Erythrosine B under the Influence of Millimeter-Range Electromagnetic Waves

• Published in: Journal of contemporary physics Vol. 58; no. 4; pp. 428 - 434
• Main Authors: Parsadanyan, M. A., Shahinyan, M. A., Grigoryan, S. V., Mikaelyan, M. S., Poghosyan, G. H., Kalantaryan, V. P., Vardevanyan, P. O.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01.12.2023; Springer Nature B.V
• Subjects: Complex formation; Denaturation; Dichroism; Electromagnetic radiation; Hydrogen bonds; Irradiation; Particle and Nuclear Physics; Physics; Physics and Astronomy; Preservatives; Serum albumin; absorption; fluorescence; binding parameters; denaturation; quenching constant; CD spectra; millimeter electromagnetic waves
• ISSN: 1068-3372; 1934-9378
• DOI: 10.1134/S106833722304014X

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.