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

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GÖKÇE B., Gencer N., Arslan O., KARATAŞ M. O. , ALICI B.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, vol.31, no.4, pp.534-537, 2016 (SCI-Expanded) identifier identifier identifier


Human serum paraoxonase 1 (PON1; EC 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 mu M) for PON1, respectively. The present study has demonstrated that PON1 activity is very highly sensitive to studied coumarin derivatives.