Akademik Veri Yönetim Sistemi
LUMINESCENCE, cilt.41, sa.5, ss.1-15, 2026 (SCI-Expanded, Scopus)
Understanding the binding mechanism of idarubicin (IDA), a chemotherapeutic agent used in the treatment of acute myeloidleukemia (AML), with bovine serum albumin (BSA) is essential for elucidating its toxicity and pharmacodynamic and pharma-cokinetic behavior and for supporting the development of novel drugs. In this study, the interaction between IDA and BSA wascomprehensively investigated using spectroscopic techniques, including steady-state fluorescence, 3D fluorescence, synchro-nous fluorescence, competitive displacement assays, UV–Vis absorption spectroscopy, and Fourier transform infrared (FT-IR)spectroscopy, along with dynamic light scattering (DLS) and molecular docking analysis. The interaction was confirmed by fluo-rescence and UV–Vis spectra, and the binding constant was determined as Ka = 1.74 × 104 M−1. Fluorescence quenching analysisindicated a predominantly static quenching mechanism, suggesting the formation of a ground-state complex. Thermodynamicresults revealed that hydrogen bonding, hydrophobic interactions, and van der Waals forces play dominant roles in the bind-ing process. Furthermore, 3D and synchronous fluorescence studies demonstrated that IDA alters the polarity of the BSA mi-croenvironment. Molecular docking and displacement studies showed that IDA binds to all three BSA sites, with a significantlyhigher affinity for Site III compared to Site I and Site II. These findings provide valuable insight into the IDA–BSA interactionmechanism.