Akademik Veri Yönetim Sistemi
Journal of Molecular Structure, cilt.1256, 2022 (SCI-Expanded)
© 2022 Elsevier B.V.The present study aims to examine fluorescence resonance energy transfer (FRET) between coumarin 151 (C151) and bovine serum albumin (BSA) in different pH mediums beside determining binding constants and energy transfer parameters using different methods considering pH levels. Once the basis of the BSA-C151 FRET system had been established, this system was designed as a new FRET-based functional chemosensory system for detection of Fe3+ ion. Fe3+ ion was observed to have specifically interacted with the system in question, thus affecting the fluorescence energy transfer between two molecules. The limit of detection (LOD) value of the system for Fe3+ ion was determined as 1.42 × 10−9 M (1.42 nM) and Fe3+concentration ranging from 10 nM to 1 μM. The molecular docking results showed that BSA had interacted with C151, which we defined as a new system. It was also revealed that BSA had interacted with two amino acid residues (Trp214 and Ser202) as a result of FeCl3 being added to the system. Beside, the in-silico studies demonstrated that the FRET occurring in the BSA-C151 system had taken place via the Trp214 amino acid residue of BSA, and that the fluorometric determination of the Fe3+ ion was based on the fluorescence quenching that occurred due to the interaction between the Trp214 amino acid residue of BSA and Fe3+ present in the BSA-C151-FeCl3 system. The BSA–C151 FRET system has good potential for Fe3+ detection in analytical systems as it shows high selectivity for Fe3+. The low LOD value in the present study also contributed to this potential.