Çinar I.Aksoy I.Güler G.2023-06-162023-06-1620209.78E+12https://doi.org/10.1109/TIPTEKNO50054.2020.9299322https://hdl.handle.net/20.500.14365/36452020 Medical Technologies Congress, TIPTEKNO 2020 -- 19 November 2020 through 20 November 2020 -- 166140Investigation of the protein-drug active substance interactions has great importance in the fields of medicine, chemistry, pharmaceutical, biomedical and toxicology. In this study, binding properties of a potential anti-cancer drug agent ifosfamide with bovine serum albumin (BSA), one of the main ligand transporters in blood plasma, was analyzed by using ultraviolet and visible light (UV-Vis) spectroscopy along with molecular docking studies. The UV-Vis spectra of the constant BSA solution (20x 10-6 M) in complexes with various concentrations of ifosfamide (20x 10-6 M to 140x 10-6 M) were obtained at physiological pH. Besides, the BSA protein was docked with ifosfamide drug active substance via computational molecular docking method. Amino acids in the binding sites of the BSA protein and the binding distances of these amino acids to the ligand (ifosfamide), their scores and RMSD values were determined, revealing that the interaction is a spontaneous process. Both molecular docking and the spectral results demonstrated that the anti-cancer drug agent binds to BSA via non-covalent interactions, resulting in minute conformational changes in BSA. © 2020 IEEE.eninfo:eu-repo/semantics/closedAccessanti-cancer drugbindingmolecular dockingproteinUV-Vis spectroscopyAmino acidsBinding energyBinding sitesBiomedical engineeringBloodDiseasesLigandsMammalsMolecular modelingpHProteinsActive substanceBinding distanceBinding propertiesBovine serum albuminsConformational changeMolecular dockingNon-covalent interactionSpontaneous processDrug interactionsConference Object10.1109/TIPTEKNO50054.2020.92993222-s2.0-85099466749