期刊
ANTIOXIDANTS
卷 11, 期 7, 页码 -出版社
MDPI
DOI: 10.3390/antiox11071245
关键词
polyphenol; thiazole; antioxidant activity; synthesis; HSA; ITC; NMR; drug binding; molecular docking
资金
- Iuliu Hatieganu University of Medicine and Pharmacy, Cluj-Napoca, Romania [35182/17.12.2021]
This study designed and synthesized a water-soluble molecule, CHT, with good antioxidant activity. The binding mechanism of CHT to human serum albumin was investigated using biophysical methods and computational studies, revealing the dominant forces involved in the binding and the enthalpy-driven nature of the process.
Polyphenols have attained pronounced attention due to their ability to provide numerous health benefits and prevent several chronic diseases. In this study, we designed, synthesized and analyzed a water-soluble molecule presenting a good antioxidant activity, namely catechol hydrazinyl-thiazole (CHT). This molecule contains 3 ',4 '-dihydroxyphenyl and 2-hydrazinyl-4-methyl-thiazole moieties linked through a hydrazone group with very good antioxidant activity in the in vitro evaluations performed. A preliminary validation of the CHT developing hypothesis was performed evaluating in silico the bond dissociation enthalpy (BDE) of the phenol O-H bonds, compared to our previous findings in the compounds previously reported by our group. In this paper, we report the binding mechanism of CHT to human serum albumin (HSA) using biophysical methods in combination with computational studies. ITC experiments reveal that the dominant forces in the binding mechanism are involved in the hydrogen bond or van der Waals interactions and that the binding was an enthalpy-driven process. NMR relaxation measurements were applied to study the CHT-protein interaction by changing the drug concentration in the solution. A molecular docking study added an additional insight to the experimental ITC and NMR analysis regarding the binding conformation of CHT to HSA.
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