R&D registration number in UkrISTEI: 0119U002038
What priority area of science and technology does it correspond to: life sciences, new technologies for the prevention and treatment of the most common diseases.
Source of funding: funds from the state budget.
Prospect for further implementation in 2021-2022: to be completed.
Research level: no analogues in Ukraine.
Brief description, advantages, further prospects for application.
The main idea of the work was to expand the possibilities of the luminescent method of analysis for determining the binding of certain drugs (LR) to human serum albumin (HSA). It was shown that LRs quench their protein fluorescence as a result of static interaction in the SAL-LR system. It has been established that quenching of luminescence is carried out due to the nonradiative transfer of electronic excitation energy (FRET) from the luminescent substance (donor) to the quencher (acceptor). Binding parameters were determined: constants, number of binding sites, and distances between the donor (NAL) and the acceptor (LR). Based on the calculated thermodynamic parameters of the binding of LR with SAL, it was found that van der Waals interactions and the formation of hydrogen bonds play an important role. A study was made of the conformational changes in LAL caused by binding to LR by measuring synchronous fluorescence spectra. It was found that for almost all LRs there are changes in the protein conformation near the tryptophan residue.
It has been shown that the intrinsic fluorescence of some LRs manifests itself in the same region of the spectrum as the intrinsic fluorescence of the protein, and therefore its emission spectrum is superimposed on the intrinsic fluorescence of the protein. In this case, for the first time, the possibility of determining the binding constants of NAL binding to drug molecules by quenching their own fluorescence was shown.