Abstract
In presented study influence of different radiation types on biosensor matrix component stability have been investigated. Conformation changes of studied protein (BSA) were monitored by UV/Vis spectra, taking into consideration absorption in 277 nm. The peak comes from the presence of aromatic residuals such as tyrosine (Tyr), phenylalanine (Phe) and (Trp) tryptophan. An increase of absorption of BSA with time has been found. It probably reflects destabilization of protein, conformational changes in the secondary structure and changes in the local environment. The effect could also be interpreted as an increase of helix conformation amount and decrease in beta sheet structure which leads to loosing of the protein skeleton. It also could indicate that fragmentation and aggregation of the investigated protein might occur with time and electrostatic interactions (ion-ion, ion-dipole, dipole-dipole interactions (van der Waals interactions)) in the protein could be changed. In the performed study, slower growth in absorption after exposition to RF electromagnetic field has been observed and effect of protein stabilization has been found. The reverse effect was perceived after exposition to VIS radiation. Comparing the trend of changes taking place over time for this two kind of radiation, it could be said that with time the differences between radiated and non-radiated samples are larger and more pronounced.
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Kłos-Witkowska, A., Martsenyuk, V. (2020). Study of Improvement of Biosensor Matrix Stability. In: Zawiślak, S., Rysiński, J. (eds) Engineer of the XXI Century. EngineerXXI 2018. Mechanisms and Machine Science, vol 70. Springer, Cham. https://doi.org/10.1007/978-3-030-13321-4_13
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