ISOFLAVANS DERIVATIVES AS INHIBITORS OF SOYBEAN LIPOXYGENASE: IN-VITRO AND DOCKING STUDIES

The lipoxygenases (LOX) are a family of non-heme iron-containing dioxygenases which catalyze the stereospecific insertion of molecular oxygen into arachidonic acid, leading to hydroxy derivatives as end products. In this work, we studied the behavior of seven isoflavans on 15-soybean lipoxygenases (15-sLOX), comparing them with the known inhibitors quercetin and 3, 4-dihydroxybenzoic acid. Four of the seven investigated isoflavans showed IC50 values smaller than 50 µM , being more potent than quercetin or 3, 4-dihydroxybenzoic acid. Besides a catecholic pattern, the presence of an aromatic ring B seems to confer additional activity to these compounds, a result which was rationalized by docking studies of these isoflavanss into the enzyme binding site.

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Main Authors: MASCAYANO,CAROLINA, CAROLI REZENDE,MARCOS, RIVERA,YENIFER, ESPINOSA,VICTORIA
Format: Digital revista
Language:English
Published: Sociedad Chilena de Química 2011
Online Access:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-97072011000400024
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spelling oai:scielo:S0717-970720110004000242012-03-06ISOFLAVANS DERIVATIVES AS INHIBITORS OF SOYBEAN LIPOXYGENASE: IN-VITRO AND DOCKING STUDIESMASCAYANO,CAROLINACAROLI REZENDE,MARCOSRIVERA,YENIFERESPINOSA,VICTORIA Soybean Lipoxygenase Isoflavans Inhibitors IC50 Values Docking The lipoxygenases (LOX) are a family of non-heme iron-containing dioxygenases which catalyze the stereospecific insertion of molecular oxygen into arachidonic acid, leading to hydroxy derivatives as end products. In this work, we studied the behavior of seven isoflavans on 15-soybean lipoxygenases (15-sLOX), comparing them with the known inhibitors quercetin and 3, 4-dihydroxybenzoic acid. Four of the seven investigated isoflavans showed IC50 values smaller than 50 µM , being more potent than quercetin or 3, 4-dihydroxybenzoic acid. Besides a catecholic pattern, the presence of an aromatic ring B seems to confer additional activity to these compounds, a result which was rationalized by docking studies of these isoflavanss into the enzyme binding site.info:eu-repo/semantics/openAccessSociedad Chilena de QuímicaJournal of the Chilean Chemical Society v.56 n.4 20112011-12-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-97072011000400024en10.4067/S0717-97072011000400024
institution SCIELO
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country Chile
countrycode CL
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databasecode rev-scielo-cl
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libraryname SciELO
language English
format Digital
author MASCAYANO,CAROLINA
CAROLI REZENDE,MARCOS
RIVERA,YENIFER
ESPINOSA,VICTORIA
spellingShingle MASCAYANO,CAROLINA
CAROLI REZENDE,MARCOS
RIVERA,YENIFER
ESPINOSA,VICTORIA
ISOFLAVANS DERIVATIVES AS INHIBITORS OF SOYBEAN LIPOXYGENASE: IN-VITRO AND DOCKING STUDIES
author_facet MASCAYANO,CAROLINA
CAROLI REZENDE,MARCOS
RIVERA,YENIFER
ESPINOSA,VICTORIA
author_sort MASCAYANO,CAROLINA
title ISOFLAVANS DERIVATIVES AS INHIBITORS OF SOYBEAN LIPOXYGENASE: IN-VITRO AND DOCKING STUDIES
title_short ISOFLAVANS DERIVATIVES AS INHIBITORS OF SOYBEAN LIPOXYGENASE: IN-VITRO AND DOCKING STUDIES
title_full ISOFLAVANS DERIVATIVES AS INHIBITORS OF SOYBEAN LIPOXYGENASE: IN-VITRO AND DOCKING STUDIES
title_fullStr ISOFLAVANS DERIVATIVES AS INHIBITORS OF SOYBEAN LIPOXYGENASE: IN-VITRO AND DOCKING STUDIES
title_full_unstemmed ISOFLAVANS DERIVATIVES AS INHIBITORS OF SOYBEAN LIPOXYGENASE: IN-VITRO AND DOCKING STUDIES
title_sort isoflavans derivatives as inhibitors of soybean lipoxygenase: in-vitro and docking studies
description The lipoxygenases (LOX) are a family of non-heme iron-containing dioxygenases which catalyze the stereospecific insertion of molecular oxygen into arachidonic acid, leading to hydroxy derivatives as end products. In this work, we studied the behavior of seven isoflavans on 15-soybean lipoxygenases (15-sLOX), comparing them with the known inhibitors quercetin and 3, 4-dihydroxybenzoic acid. Four of the seven investigated isoflavans showed IC50 values smaller than 50 µM , being more potent than quercetin or 3, 4-dihydroxybenzoic acid. Besides a catecholic pattern, the presence of an aromatic ring B seems to confer additional activity to these compounds, a result which was rationalized by docking studies of these isoflavanss into the enzyme binding site.
publisher Sociedad Chilena de Química
publishDate 2011
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-97072011000400024
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