Study of thermal stability of bovine serum albumin under the non-heating alternating magnetic field treatment

Abstract

The functional integrity of proteins directly depends on their structural stability. he presence of a denaturing agent. Reversible and irreversible denaturation are also distinguished. The conformational stability of the protein in the study can be assessed using the natural fluorescence of tryptophan with an excitation maximum at 280 nm and an emission maximum at 320-375 nm. Tryptophan fluorescence can be detected using the nanoDSF method - nano-differential scanning fluorimetry. The objects of the study were lysozyme and bovine serum albumin (BSA). Deionized water, phosphate-buffered saline (PBS), acetate buffer. The study was carried out using a multifunctional protein stability analyzer PSA-16 (Bestscience&technology, Beijing, China).
From the obtained data it can be concluded that lysozyme is more stable in PBS and HEPES, BSA is also more stable in PBS. 0.5 mg/ml BSA denatures and decomposes more slowly than 1.0 mg/ml BSA. Thermal stability of BSA was analyzed after exposure to an alternating magnetic field (100 mT, 17, 34, 48, 95 Hz, 10 min) and ultrasound (60% power, 15, 30, 45, 60 s). The melting temperature of the protein does not change in any way depending on the exposure conditions. Samples exposed to magnetic action were studied for isothermal stability for 24 h. In the presence of short-term areas of decreased fluorescence, the curves returned to the previous intensity value.
The work was carried out within the framework of the RSF project 23-13-00373 «Mechanism of antitumor action of an alternating non-heating magnetic field in vitro and in vivo».

Speaker

Alexandra E. Kalinova
Federal State Budgetary Educational Institution of Higher Education "Saratov National Research State University named after N.G. Chernyshevsky" Institute of Physics, Saratov, Russia
Russian Federation

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