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

Authors :: Gokce B
Gencer N
Arslan O
Karatas MO
Alici B
Source :: Journal of enzyme inhibition and medicinal chemistry [J Enzyme Inhib Med Chem] 2016 Aug; Vol. 31 (4), pp. 534-7. Date of Electronic Publication: 2015 May 18.
Publication Year :: 2016
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.

Subjects :: Aryldialkylphosphatase isolation & purification
Aryldialkylphosphatase metabolism
Coumarins chemical synthesis
Coumarins chemistry
Dose-Response Relationship, Drug
Enzyme Inhibitors chemical synthesis
Enzyme Inhibitors chemistry
Humans
Inhibitory Concentration 50
Molecular Structure
Structure-Activity Relationship
Aryldialkylphosphatase antagonists & inhibitors
Coumarins pharmacology
Enzyme Inhibitors pharmacology

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