Interaction of 3-(1H-tetrazol-5-yl) Coumarin With Bovine Serum Albumin and Calf Thymus DNA: Deciphering the Mode of Binding by In Vitro Studies

Background: Coumarins comprise a large family of heterocyclic compounds with benzo-a-pyrone moiety. Objectives: This study aimed to analyze the binding affinity 3-(1H-tetrazol-5-yl) coumarin bovine serum albumin (BSA) and calf thymus DNA (Ct-DNA) using fluorescence spectroscopy. The quenching was recognized during interaction between BSA, followed by static mechanism. Methods: hydrogen bonds, hydrophobic interactions, Vander Waals forces were regarded as principal part in BSA complexation process. spectral characteristics demonstrated an enhancement intensity presence ct-DNA solution. Results: experimental results indicated that binds via interjection, forces. work illustrated quenched mechanism secondary structure proteins changed upon drug binding. Conclusion: It is deduced represents higher compared BSA. finding can be useful designing more effective new drugs fewer side effects.