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

GÖKÇE B., GENÇER 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

  • Publication Type: Article / Article
  • Volume: 31 Issue: 4
  • Publication Date: 2016
  • Doi Number: 10.3109/14756366.2015.1043297
  • Journal Name: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.534-537
  • Keywords: Coumarin derivatives, in vitro inhibition, paraoxonase, PURIFICATION, DERIVATIVES, METABOLISM, TOXICITY, EFFICACY, SAFETY
  • Inonu University Affiliated: Yes

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 mu M) for PON1, respectively. The present study has demonstrated that PON1 activity is very highly sensitive to studied coumarin derivatives.