SPECTROSCOPIC EVALUATION OF THE INTERACTION OF A TETRAZOLE DERIVATIVE SYNTHESIZED BY SEMI-GREEN METHOD WITH CALF THYMUS DNA AND BOVINE SERUM PROTEIN

Authors

  • Sargolzaei, Javad Department of Biology, Faculty of Science, Arak University, Arak, Iran (Corresponding Author)
Abstract:

Background & Aims: In recent decades, the application of tetrazole structures in various fields of medicine and industry has become very important, because they can cause structural and thus functional changes in the proteins. In this article, the effect of a new tetrazole derivative on calf thymus DNA (Ct-DNA) as well as on bovine serum albumin protein (BSA) in the solution was determined using various spectroscopic methods in vitro. Materials & Methods: The primary, secondary, and tertiary structures of BSA proteins and Ct-DNA were studied using UV-Vis spectroscopy, circular dichroism (CD), and fluorescence spectroscopy, respectively. Results: The results showed that the optical density of Ct-DNA and BSA were increased in the resukt of interactions with oxindolin-(H1-tetrazol-5-yl) acetonitrile at 260 and 280 nm. The emission spectra of Ct-DNA and BSA decreased dependent to the concentration of oxindolin-(H1-tetrazol-5-yl) acetonitrile, which indicates the binding of oxindolin-(H1-tetrazol-5-yl) acetonitrile to chromophores in Ct-DNA and BSA. Binding of oxindolin-(H1-tetrazol-5-yl) acetonitrile causes a significant increase in ellipticity, circular dichroism of DNA molecules in the regions of 220 and 275 nm, and increase in its negativity in 245 nm, which shows an stronger binding of oxindolin- (H1-tetrazol-5-yl) acetonitrile to Ct-DNA. As the concentration increases, the molar ellipse associated with the alpha helix in the BSA structure becomes more negative in the 220 nm region, which indicates an increase in the amount of irregular coils in the structure of BSA. Conclusion: The obtained results can provide useful information in the field of designing drugs with tetrazole derivatives with more anti-tumor effect and less side effects.

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Journal title

volume 33  issue 6

pages  392- 403

publication date 2022-09

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