Events9th International Electronic Conference on Medicinal Chemistry
Published
with-doi10.3390/ECMC2023-15703 (registering DOI)
This submission belongs to the session S4. New Small molecules as drug candidates of the event 9th International Electronic Conference on Medicinal Chemistry
Published date
01 Nov, 2023
Academic Editor
author-avatarMaria Emília Sousa
Citation
Miloš Nikolić, Nikola Nedeljković, Ratomir Jelić, Emina Mrkalić, Gordana Radić, Zoran Ratković, Andriana Bukonjić, Investigation of the interaction between isopropyl derivative of thiosalicylic acid and human serum albumin, in Proceedings of 9th International Electronic Conference on Medicinal Chemistry, 1 November–30 November 2023, MDPI: Basel, Switzerland, doi: 10.3390/ECMC2023-15703
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Investigation of the interaction between isopropyl derivative of thiosalicylic acid and human serum albumin

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Zoran Ratković 3
Andriana Bukonjić 1
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1. University of Kragujevac, Faculty of Medical Sciences, Department of Pharmacy, Svetozara Markovića 69, 34000 Kragujevac, Serbia, Serbia
2. University of Kragujevac, Institute for Information Technologies, Department of Science, Jovana Cvijića bb, Kragujevac 34000, Serbia, Serbia
3. University of Kragujevac, Faculty of Science, Department of Chemistry, Radoja Domanovića 12, Kragujevac 34000, Serbia, Serbia
Abstract

According to research, thiosalicylic acid has anti-inflammatory, antioxidant, and analgesic effects. Additionally, some of its derivatives have shown significant antimicrobial and antitumor activity. In vitro studies have also shown that S-alkyl derivatives of thiosalicylic acid exhibit moderate and dose-dependent cytotoxic effects on human colon and lung carcinoma cells. In this reserach, we utilized various spectroscopic methods and molecular docking simulation to examine the binding interaction between human serum albumin (HSA) and potential biologically active isopropyl derivatives of thiosalicylic acid (ligand, L). To analyze the quenching mechanism, the association constants and number of binding sites were utilized based on the obtained results. The tested L and HSA had a static fluorescence quenching mechanism, while their binding processes were spontaneous. Additionally, UV-Vis absorption spectroscopy revealed that the binding of the tested L induced slight conformational changes in HSA.

Keywords
Human serum albumin
Thiosalicylic acid
Spectroscopic measurements
Docking simulations
Manuscript
Evaluation of in vitro cytotoxic and hemolytic effects of a new series of hydroxy- and nitro-containing arylcoumarins
Investigation of binding mode of isoamyl derivative of thiosalicylic acid and human serum albumin