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 a benzo-a-pyrone moiety. objectives: this study aimed to analyze the binding affinity of 3-(1h-tetrazol-5-yl) coumarin to bovine serum albumin (bsa) and calf thymus dna (ct-dna) using fluorescence spectroscopy. the quenching of fluorescence was recognized during the interaction between 3-(1h-tetrazol-5-yl) coumarin and bsa, followed by a static mechanism. methods: the hydrogen bonds, hydrophobic interactions, and vander waals forces were regarded as the principal part in the 3-(1h-tetrazol-5-yl) coumarin and bsa complexation process. the fluorescence spectral characteristics demonstrated an enhancement in fluorescence intensity of the 3-(1h-tetrazol-5-yl) coumarin in the presence of ct-dna solution. results: the experimental results indicated that the 3-(1h-tetrazol-5-yl) coumarin binds to dna via interjection, hydrogen bonds, and vander waals forces. this work illustrated that bsa fluorescence was quenched by 3-(1h-tetrazol-5-yl) coumarin via a static mechanism and the ct-dna fluorescence enhancement by 3-(1h-tetrazol-5-yl) coumarin was a static process. the secondary structure of proteins changed upon drug binding. conclusion: it is deduced that 3-(1h-tetrazol-5-yl) coumarin represents a higher binding affinity to dna compared to bsa. this finding can be useful in designing more effective new drugs with fewer side effects.