Kazici, DilekAlagoz, Mehmet AbdullahSavan, Ebru Kuyumcu2024-08-042024-08-0420222299-680Xhttps://doi.org/10.37819/nanofab.007.225https://hdl.handle.net/11616/103037The binding ability of the drug on its interaction with the protein will also significantly affect the apparent volume of distribution of the drugs and, in many cases the rate of elimination of the drugs. The interactions of proteins and other molecules are a fascinating topic applied to surface technologies and sensors. Therefore, it is aimed to determine the NBTCand to elucidate its interaction with Bovine Serum Albumin (BSA) by electrochemical and in silico studies in this paper. The reduction in BSA oxidation signals measured by differential pulse voltammetry upon incubation with different NBTC concentrations indicated that NBTC was bound to BSA. In addition, in silico (molecular modeling and molecular dynamics) studies have been conducted on the interactions of NBTC with proteins in plasma. As a result of the in silico studies investigated the interactions of NBTC with serum albumin, its binding affinity, and the dynamic process in the binding state. In silico studies showed that NBTC binds to BSA with high affinity (with-7.986 kcal/mol docking score), and this binding was stable (with a 3.0 average RMSD value). Eventually, the results of the electrochemical and modeling studies were perfectly matched.eninfo:eu-repo/semantics/openAccessNitro Blue Tetrazolium ChlorideBovine Serum Albuminin SilicoVoltammetryArticle7212110.37819/nanofab.007.225WOS:000919670600005N/A