ACCELERATED HEMOGLOBIN DENATURATION IN PHYSIOLOGICAL SOLUTIONSTHAT WERE PRE-EXPOSED TO IONIZING RADIATION
DOI:
https://doi.org/10.17721/1728.2748.2026.105.43-48Keywords:
ionizing radiation, physiological solution, hemoglobin, denaturation, pH, water radiolysis, nanobubblesAbstract
Background. This study investigates the impact of low doses of ionizing radiation (equivalent to the background radiation levels on space stations) on the properties of 0.9 % NaCl physiological solutions. The relevance of this research is driven by the need to assess the stability of pharmaceuticals and proteins in environments subjected to long-term radiation exposure, as water radiolysis can significantly alter their physicochemical state. Hemoglobin, specifically its optical properties, was used as a marker for the redox and acidic state of the medium.
Methods. The study utilized 0.9% NaCl solution in ampoules, irradiated with 241Am, 239Pu-9Be and 137Cs sources (dose rates of 10–14 μSv/h) for durations of 21 and 57 days. Concentrated rat hemoglobin solution was added to these pre-irradiated physiological solutions. The optical properties of the samples were monitored via spectrophotometry during 120 hours of storage at 21–22 °C.
Results. Irradiation of the physiological solutions was found to cause a consistent decrease in light scattering within the UV range, indicating the destabilization or size reduction of gas nanobubbles. Hemoglobin in control solutions remained stable during the first 24 hours, whereas an accelerated degradation of its spatial structure was observed in the pre-irradiated solutions. By the 120-hour mark, the protein in all experimental samples had transitioned into a denatured state (methemoglobin, Fe3+). This process was accompanied by a "blue shift" of the Soret band by 6–8 nm and the disappearance of the absorption maxima at 540 and 575 nm, which are characteristic of the native oxygenated form of the protein.
Conclusions. The primary causes of accelerated protein denaturation are the acidification of the medium (a pH decrease of 0.3–0.5 units) resulting from water radiolysis, and the formation of reactive oxygen species and oxidants (hypochlorites, chlorites, chlorates). A separate control experiment with HCl confirmed that a low pH (4.0) triggers rapid hemoglobin degradation within 15 minutes, with corresponding changes in the optical properties of the protein solutions. Thus, prolonged exposure even to low doses of radiation markedly alters the physicochemical properties of physiological solutions, which critically affects the stability of dissolved proteins.
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