In vitro inhibition effect of some coumarin compounds on purified human serum paraoxonase 1 (PON1)

Abstract

Human serum paraoxonase 1 (PON1; EC 3.1.8.1) is a high-density lipoprotein associated, calcium-dependent enzyme that hydrolyses aromatic esters, organophosphates and lactones and can protect the low-density lipoprotein against oxidation. In this study, in vitro effect of some hydroxy and dihydroxy ionic coumarin derivatives (1–20) on purified PON1 activity was investigated. Among these compounds, derivatives 11–20 are water soluble. In investigated compounds, compounds 6 and 13 were found the most active (IC₅₀ = 35 and 34 µM) for PON1, respectively. The present study has demonstrated that PON1 activity is very highly sensitive to studied coumarin derivatives.

• Coumarin derivatives
• in vitro inhibition
• paraoxonase

Acknowledgements

The authors would like to thank Fehim İlhan for his advice on English grammar and expression.

Declaration of interest

This work has been supported by Balikesir University Research project (2014/54).