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Soheila Khaghaninejad

Soheila Khaghaninejad

Academic rank: Assistant Professor
ORCID: https://orcid.org/0009-0002-2160-9774
Faculty: Science
Address: Arak University
Phone: 08632627510


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
3-(1H-tetrazol-5-yl) coumarin, Bovine serum albumin, Calf thymus DNA (Ct-DNA), Binding, Spectroscopy
Journal Avicenna Journal of Medical Biochemistry
Researchers Javad Sargolzaei ، Soheila Khaghaninejad


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