title: Investigation of Mammal Arginase Inhibitory Properties of Natural Ubiquitous Polyphenols by Using an Optimized Colorimetric Microplate Assay.
abstract: Polyphenols are plant secondary metabolites which possess many positive effects on human health. Although these beneficial effects could be mediated through an increase in nitric oxide synthase activity, little is known regarding the inhibitory effect of polyphenols on mammal arginase, an enzyme which competes with nitric oxide synthase for their common substrate, L-arginine. The aim of the present study was to determine the potential of a series of polyphenols as mammalian arginase inhibitors and to identify some structure-activity relationships. For this purpose, we first developed a simple and cost-effectivein vitrocolorimetric microplate method using commercially-available mammal bovine liver arginase (b-ARG 1). Among the ten tested polyphenolic compounds [chlorogenic acid, piceatannol, resveratrol, (-)-epicatechin, taxifolin, quercetin, fisetin, caffeic acid, quinic acid, and kaempferol], cholorogenic acid and piceatannol exhibited the highest inhibitory activities (IC50= 10.6 and 12.1 µM, respectively) but were however less active as (S)-(2-Boronoethyl)-L-cysteine (IC50= 3.3 µM), used as reference compound. Enzyme kinetic studies showed that both chlorogenic acid and piceatannol are competitive arginase inhibitors. Structural data identified the importance of the caffeoyl (3,4-dihydroxycinnamoyl)-part and of the catechol function in the inhibitory activity of the tested compounds. These results identified chlorogenic acid and piceatannol as two potential core structures for the design of new arginase inhibitors.
authors: PEPITE EA4267, Univ. Bourgogne Franche-Comté, Besançon, France.
authors: Simon
authors: S
authors: Bordage
authors: PEPITE EA4267, Univ. Bourgogne Franche-Comté, Besançon, France.
authors: Thanh-Nhat
authors: TN
authors: Pham
authors: PEPITE EA4267, Univ. Bourgogne Franche-Comté, Besançon, France.
authors: Andy
authors: A
authors: Zedet
authors: PEPITE EA4267, Univ. Bourgogne Franche-Comté, Besançon, France.
authors: Anne-Sophie
authors: AS
authors: Gugglielmetti
authors: PEPITE EA4267, Univ. Bourgogne Franche-Comté, Besançon, France.
authors: Maude
authors: M
authors: Nappey
authors: PEPITE EA4267, Univ. Bourgogne Franche-Comté, Besançon, France.
authors: Céline
authors: C
authors: Demougeot
authors: PEPITE EA4267, Univ. Bourgogne Franche-Comté, Besançon, France.
authors: Corine
authors: C
authors: Girard-Thernier
mesh_terms: D000818:Animals; D001119:Arginase / Q000037:antagonists & inhibitors*; D002417:Cattle; D003124:Colorimetry / Q000379:methods*; D059808:Polyphenols / Q000737:chemistry / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D059808:Polyphenols; D001119:Arginase