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Submitted: 16 Jul 2022
Revision: 08 Sep 2022
Accepted: 18 Sep 2022
ePublished: 19 Dec 2022
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Avicenna J Med Biochem. 2022;10(2): 153-161.
doi: 10.34172/ajmb.2022.2374
  Abstract View: 511
  PDF Download: 236

Original Article

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

Javad Sargolzaei 1* ORCID logo, Soheila Khaghaninejad 2,3, Sogol Meknatkhah 4

1 Department of Biology, Faculty of Science, Arak University, Arak, Iran
2 Department of Chemistry, Faculty of Science, Arak University, Arak, Iran
3 Institute of Nanosciences and Nanotechnology, Arak University, Arak, Iran
4 Department of Biochemistry, Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
*Corresponding Author: Corresponding author: Javad Sargolzaei, Email: , Email: j-sargolzaei@araku.ac.ir

Abstract

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.


Please cite this article as follows: Sargolzaei J, Khaghaninejad S, Meknatkhah S. 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. Avicenna J Med Biochem. 2022; 10(2):153-161. doi:10.34172/ajmb.2022.2374
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