Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitor
Apocynin is the most employed inhibitor of NADPH oxidase (NOX), a multienzymatic complex capable of catalyzing the one-electron reduction of molecular oxygen to the superoxide anion. Despite controversies about its selectivity, apocynin has been used as one of the most promising drugs in experimenta...
| Autores: | , , , |
|---|---|
| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2013 |
| País: | Brasil |
| Recursos: | Universidade Estadual Paulista (UNESP) |
| Repositorio: | Repositório Institucional da UNESP |
| Idioma: | inglés |
| OAI Identifier: | oai:repositorio.unesp.br:11449/74759 |
| Acesso em linha: | http://dx.doi.org/10.3390/molecules18032821 http://hdl.handle.net/11449/74759 |
| Access Level: | acceso abierto |
| Palavra-chave: | Albumin Apocynin Binding constant Hydrogen peroxide NADPH oxidase acetophenone derivative apocynin enzyme inhibitor hydrogen peroxide hypochlorous acid reduced nicotinamide adenine dinucleotide phosphate oxidase scavenger chemical phenomena chemistry drug antagonism kinetics oxidation reduction reaction pH Acetophenones Enzyme Inhibitors Free Radical Scavengers Hydrogen Peroxide Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Hypochlorous Acid Kinetics NADPH Oxidase Oxidation-Reduction |
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| dc.title.none.fl_str_mv |
Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitor |
| title |
Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitor |
| spellingShingle |
Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitor Petrônio, Maicon S. [UNESP] Albumin Apocynin Binding constant Hydrogen peroxide NADPH oxidase acetophenone derivative apocynin enzyme inhibitor hydrogen peroxide hypochlorous acid reduced nicotinamide adenine dinucleotide phosphate oxidase scavenger chemical phenomena chemistry drug antagonism kinetics oxidation reduction reaction pH Acetophenones Enzyme Inhibitors Free Radical Scavengers Hydrogen Peroxide Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Hypochlorous Acid Kinetics NADPH Oxidase Oxidation-Reduction |
| title_short |
Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitor |
| title_full |
Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitor |
| title_fullStr |
Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitor |
| title_full_unstemmed |
Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitor |
| title_sort |
Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitor |
| dc.creator.none.fl_str_mv |
Petrônio, Maicon S. [UNESP] Zeraik, Maria Luiza [UNESP] Da Fonseca, Luiz Marcos [UNESP] Ximenes, Valdecir F. [UNESP] |
| author |
Petrônio, Maicon S. [UNESP] |
| author_facet |
Petrônio, Maicon S. [UNESP] Zeraik, Maria Luiza [UNESP] Da Fonseca, Luiz Marcos [UNESP] Ximenes, Valdecir F. [UNESP] |
| author_role |
author |
| author2 |
Zeraik, Maria Luiza [UNESP] Da Fonseca, Luiz Marcos [UNESP] Ximenes, Valdecir F. [UNESP] |
| author2_role |
author author author |
| dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) |
| dc.subject.por.fl_str_mv |
Albumin Apocynin Binding constant Hydrogen peroxide NADPH oxidase acetophenone derivative apocynin enzyme inhibitor hydrogen peroxide hypochlorous acid reduced nicotinamide adenine dinucleotide phosphate oxidase scavenger chemical phenomena chemistry drug antagonism kinetics oxidation reduction reaction pH Acetophenones Enzyme Inhibitors Free Radical Scavengers Hydrogen Peroxide Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Hypochlorous Acid Kinetics NADPH Oxidase Oxidation-Reduction |
| topic |
Albumin Apocynin Binding constant Hydrogen peroxide NADPH oxidase acetophenone derivative apocynin enzyme inhibitor hydrogen peroxide hypochlorous acid reduced nicotinamide adenine dinucleotide phosphate oxidase scavenger chemical phenomena chemistry drug antagonism kinetics oxidation reduction reaction pH Acetophenones Enzyme Inhibitors Free Radical Scavengers Hydrogen Peroxide Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Hypochlorous Acid Kinetics NADPH Oxidase Oxidation-Reduction |
| description |
Apocynin is the most employed inhibitor of NADPH oxidase (NOX), a multienzymatic complex capable of catalyzing the one-electron reduction of molecular oxygen to the superoxide anion. Despite controversies about its selectivity, apocynin has been used as one of the most promising drugs in experimental models of inflammatory and neurodegenerative diseases. Here, we aimed to study the chemical and biophysical properties of apocynin. The oxidation potential was determined by cyclic voltammetry (Epa = 0.76V), the hydrophobicity index was calculated (logP = 0.83) and the molar absorption coefficient was determined (ε275nm = 1.1 × 104 M-1 cm-1). Apocynin was a weak free radical scavenger (as measured using the DPPH, peroxyl radical and nitric oxide assays) when compared to protocatechuic acid, used here as a reference antioxidant. On the other hand, apocynin was more effective than protocatechuic acid as scavenger of the non-radical species hypochlorous acid. Apocynin reacted promptly with the non-radical reactive species H2O2 only in the presence of peroxidase. This finding is relevant, since it represents a new pathway for depleting H2O2 in cellular experimental models, besides the direct inhibition of NADPH oxidase. This could be relevant for its application as an inhibitor of NOX4, since this isoform produces H 2O2 and not superoxide anion. The binding parameters calculated by fluorescence quenching showed that apocynin binds to human serum albumin (HSA) with a binding affinity of 2.19 × 104 M -1. The association did not alter the secondary and tertiary structure of HSA, as verified by synchronous fluorescence and circular dichroism. The displacement of fluorescent probes suggested that apocynin binds to site I and site II of HSA. Considering the current biomedical applications of this phytochemical, the dissemination of these chemical and biophysical properties can be very helpful for scientists and physicians interested in the use of apocynin. |
| publishDate |
2013 |
| dc.date.none.fl_str_mv |
2013-03-01 2014-05-27T11:28:37Z 2014-05-27T11:28:37Z |
| dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
| dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.3390/molecules18032821 Molecules, v. 18, n. 3, p. 2821-2839, 2013. 1420-3049 http://hdl.handle.net/11449/74759 10.3390/molecules18032821 WOS:000316611700028 2-s2.0-84875625176 2-s2.0-84875625176.pdf |
| url |
http://dx.doi.org/10.3390/molecules18032821 http://hdl.handle.net/11449/74759 |
| identifier_str_mv |
Molecules, v. 18, n. 3, p. 2821-2839, 2013. 1420-3049 10.3390/molecules18032821 WOS:000316611700028 2-s2.0-84875625176 2-s2.0-84875625176.pdf |
| dc.language.iso.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
Molecules 3.098 0,855 |
| dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
| eu_rights_str_mv |
openAccess |
| dc.format.none.fl_str_mv |
2821-2839 application/pdf |
| dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
| instname_str |
Universidade Estadual Paulista (UNESP) |
| instacron_str |
UNESP |
| institution |
UNESP |
| reponame_str |
Repositório Institucional da UNESP |
| collection |
Repositório Institucional da UNESP |
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Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
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repositoriounesp@unesp.br |
| _version_ |
1853671482288242688 |
| spelling |
Apocynin: Chemical and biophysical properties of a NADPH oxidase inhibitorAlbuminApocyninBinding constantHydrogen peroxideNADPH oxidaseacetophenone derivativeapocyninenzyme inhibitorhydrogen peroxidehypochlorous acidreduced nicotinamide adenine dinucleotide phosphate oxidasescavengerchemical phenomenachemistrydrug antagonismkineticsoxidation reduction reactionpHAcetophenonesEnzyme InhibitorsFree Radical ScavengersHydrogen PeroxideHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsHypochlorous AcidKineticsNADPH OxidaseOxidation-ReductionApocynin is the most employed inhibitor of NADPH oxidase (NOX), a multienzymatic complex capable of catalyzing the one-electron reduction of molecular oxygen to the superoxide anion. Despite controversies about its selectivity, apocynin has been used as one of the most promising drugs in experimental models of inflammatory and neurodegenerative diseases. Here, we aimed to study the chemical and biophysical properties of apocynin. The oxidation potential was determined by cyclic voltammetry (Epa = 0.76V), the hydrophobicity index was calculated (logP = 0.83) and the molar absorption coefficient was determined (ε275nm = 1.1 × 104 M-1 cm-1). Apocynin was a weak free radical scavenger (as measured using the DPPH, peroxyl radical and nitric oxide assays) when compared to protocatechuic acid, used here as a reference antioxidant. On the other hand, apocynin was more effective than protocatechuic acid as scavenger of the non-radical species hypochlorous acid. Apocynin reacted promptly with the non-radical reactive species H2O2 only in the presence of peroxidase. This finding is relevant, since it represents a new pathway for depleting H2O2 in cellular experimental models, besides the direct inhibition of NADPH oxidase. This could be relevant for its application as an inhibitor of NOX4, since this isoform produces H 2O2 and not superoxide anion. The binding parameters calculated by fluorescence quenching showed that apocynin binds to human serum albumin (HSA) with a binding affinity of 2.19 × 104 M -1. The association did not alter the secondary and tertiary structure of HSA, as verified by synchronous fluorescence and circular dichroism. The displacement of fluorescent probes suggested that apocynin binds to site I and site II of HSA. Considering the current biomedical applications of this phytochemical, the dissemination of these chemical and biophysical properties can be very helpful for scientists and physicians interested in the use of apocynin.Departamento de Análises Clínicas Faculdade de Ciências Farmacêuticas Unesp-Univ Estadual Paulista, Araraquara, SP 14801-902Departamento de Química Orgânica Instituto de Química Unesp-Univ Estadual Paulista, Araraquara, SP, 14800-900Departamento de Química Faculdade de Ciências Unesp-Univ Estadual Paulista, Bauru, SP 17033-360Departamento de Análises Clínicas Faculdade de Ciências Farmacêuticas Unesp-Univ Estadual Paulista, Araraquara, SP 14801-902Departamento de Química Orgânica Instituto de Química Unesp-Univ Estadual Paulista, Araraquara, SP, 14800-900Departamento de Química Faculdade de Ciências Unesp-Univ Estadual Paulista, Bauru, SP 17033-360Universidade Estadual Paulista (Unesp)2014-05-27T11:28:37Z2014-05-27T11:28:37Z2013-03-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article2821-2839application/pdfhttp://dx.doi.org/10.3390/molecules18032821Molecules, v. 18, n. 3, p. 2821-2839, 2013.1420-3049http://hdl.handle.net/11449/7475910.3390/molecules18032821WOS:0003166117000282-s2.0-848756251762-s2.0-84875625176.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengMolecules3.0980,855info:eu-repo/semantics/openAccessPetrônio, Maicon S. [UNESP]Zeraik, Maria Luiza [UNESP]Da Fonseca, Luiz Marcos [UNESP]Ximenes, Valdecir F. [UNESP]2025-06-24T05:04:27Zoai:repositorio.unesp.br:11449/74759Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestrepositoriounesp@unesp.bropendoar:29462025-06-24T05:04:27Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
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15.301629 |