Methyl divanillate: Redox properties and binding affinity with albumin of an antioxidant and potential NADPH oxidase inhibitor
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1039/c9ra02465d http://hdl.handle.net/11449/190467 |
Resumo: | Vanillic acid is a widely used food additive (flavouring agent, JECFA number: 959) with many reported beneficial biological effects. The same is true for its ester derivative (methyl vanillate, JECFA number: 159). Based on the increasing evidence that diapocynin, the dimer of apocynin (NADPH oxidase inhibitor), has some improved pharmacological properties compared to its monomer, here the dimer of methyl vanillate (MV), i.e., methyl divanillate (dimer of methyl vanillate, DMV) was synthesized and studied in the context of its redox properties and binding affinity with human serum albumin (HSA). We found that the antioxidant potency of DMV was significantly increased compared to MV. In this regard, the reduction of 2,2-diphenyl-1-picrylhydrazyl (DPPH) free radical by DMV was 30-fold more effective compared to MV. Ferric ion reduction was 4-fold higher and peroxyl radical reduction was 2.7-fold higher. The interaction with HSA was significantly improved (Stern-Vomer constants, 3.8 × 105 mol-1 L and 2.3 × 104 mol-1 L, for DMV and MV, respectively). The complexation between DMV and HSA was also evidenced by induced circular dichroism (ICD) signal generation in the former due to its fixation in the asymmetric protein pocket. Density-functional calculations (TD-DFT) showed that the ICD spectrum was related to a DMV conformation bearing a dihedral angle of approximately -60°. Similar dihedral angles were obtained in the lowest and most populated DMV cluster poses obtained by molecular docking simulations. The computational studies and experimental displacement studies revealed that DMV binds preferentially at site I. In conclusion, besides being a powerful antioxidant, DMV is also a strong ligand of HSA. This is the first study on the chemical and biophysical properties of DMV, a compound with potential beneficial biological effects. |
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Methyl divanillate: Redox properties and binding affinity with albumin of an antioxidant and potential NADPH oxidase inhibitorVanillic acid is a widely used food additive (flavouring agent, JECFA number: 959) with many reported beneficial biological effects. The same is true for its ester derivative (methyl vanillate, JECFA number: 159). Based on the increasing evidence that diapocynin, the dimer of apocynin (NADPH oxidase inhibitor), has some improved pharmacological properties compared to its monomer, here the dimer of methyl vanillate (MV), i.e., methyl divanillate (dimer of methyl vanillate, DMV) was synthesized and studied in the context of its redox properties and binding affinity with human serum albumin (HSA). We found that the antioxidant potency of DMV was significantly increased compared to MV. In this regard, the reduction of 2,2-diphenyl-1-picrylhydrazyl (DPPH) free radical by DMV was 30-fold more effective compared to MV. Ferric ion reduction was 4-fold higher and peroxyl radical reduction was 2.7-fold higher. The interaction with HSA was significantly improved (Stern-Vomer constants, 3.8 × 105 mol-1 L and 2.3 × 104 mol-1 L, for DMV and MV, respectively). The complexation between DMV and HSA was also evidenced by induced circular dichroism (ICD) signal generation in the former due to its fixation in the asymmetric protein pocket. Density-functional calculations (TD-DFT) showed that the ICD spectrum was related to a DMV conformation bearing a dihedral angle of approximately -60°. Similar dihedral angles were obtained in the lowest and most populated DMV cluster poses obtained by molecular docking simulations. The computational studies and experimental displacement studies revealed that DMV binds preferentially at site I. In conclusion, besides being a powerful antioxidant, DMV is also a strong ligand of HSA. This is the first study on the chemical and biophysical properties of DMV, a compound with potential beneficial biological effects.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Department of Chemistry Faculty of Sciences UNESP-São Paulo State UniversityLaboratory of Computational Biology and Bioinformatics UFABC-Federal University of ABCDepartment of Physical Chemistry Institute of Chemistry Campinas State University (UNICAMP)Department of Chemistry Faculty of Sciences UNESP-São Paulo State UniversityFAPESP: 2014/50926-0FAPESP: 2016/20549-5FAPESP: 2016/22014-1CNPq: 302793/2016-0CNPq: 305541/2017-0Universidade Estadual Paulista (Unesp)Universidade Federal do ABC (UFABC)Universidade Estadual de Campinas (UNICAMP)De Vasconcelos, Debora Naliati [UNESP]Lima, Angélica NakagawaPhilot, Eric AllisonScott, Ana LígiaFerreira Boza, Izabelle Amorim [UNESP]De Souza, Aguinaldo Robinson [UNESP]Morgon, Nelson HenriqueXimenes, Valdecir Farias [UNESP]2019-10-06T17:14:12Z2019-10-06T17:14:12Z2019-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article19983-19992http://dx.doi.org/10.1039/c9ra02465dRSC Advances, v. 9, n. 35, p. 19983-19992, 2019.2046-2069http://hdl.handle.net/11449/19046710.1039/c9ra02465d2-s2.0-85068367817Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengRSC Advancesinfo:eu-repo/semantics/openAccess2024-04-29T18:17:13Zoai:repositorio.unesp.br:11449/190467Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-04-29T18:17:13Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Methyl divanillate: Redox properties and binding affinity with albumin of an antioxidant and potential NADPH oxidase inhibitor |
title |
Methyl divanillate: Redox properties and binding affinity with albumin of an antioxidant and potential NADPH oxidase inhibitor |
spellingShingle |
Methyl divanillate: Redox properties and binding affinity with albumin of an antioxidant and potential NADPH oxidase inhibitor De Vasconcelos, Debora Naliati [UNESP] |
title_short |
Methyl divanillate: Redox properties and binding affinity with albumin of an antioxidant and potential NADPH oxidase inhibitor |
title_full |
Methyl divanillate: Redox properties and binding affinity with albumin of an antioxidant and potential NADPH oxidase inhibitor |
title_fullStr |
Methyl divanillate: Redox properties and binding affinity with albumin of an antioxidant and potential NADPH oxidase inhibitor |
title_full_unstemmed |
Methyl divanillate: Redox properties and binding affinity with albumin of an antioxidant and potential NADPH oxidase inhibitor |
title_sort |
Methyl divanillate: Redox properties and binding affinity with albumin of an antioxidant and potential NADPH oxidase inhibitor |
author |
De Vasconcelos, Debora Naliati [UNESP] |
author_facet |
De Vasconcelos, Debora Naliati [UNESP] Lima, Angélica Nakagawa Philot, Eric Allison Scott, Ana Lígia Ferreira Boza, Izabelle Amorim [UNESP] De Souza, Aguinaldo Robinson [UNESP] Morgon, Nelson Henrique Ximenes, Valdecir Farias [UNESP] |
author_role |
author |
author2 |
Lima, Angélica Nakagawa Philot, Eric Allison Scott, Ana Lígia Ferreira Boza, Izabelle Amorim [UNESP] De Souza, Aguinaldo Robinson [UNESP] Morgon, Nelson Henrique Ximenes, Valdecir Farias [UNESP] |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidade Federal do ABC (UFABC) Universidade Estadual de Campinas (UNICAMP) |
dc.contributor.author.fl_str_mv |
De Vasconcelos, Debora Naliati [UNESP] Lima, Angélica Nakagawa Philot, Eric Allison Scott, Ana Lígia Ferreira Boza, Izabelle Amorim [UNESP] De Souza, Aguinaldo Robinson [UNESP] Morgon, Nelson Henrique Ximenes, Valdecir Farias [UNESP] |
description |
Vanillic acid is a widely used food additive (flavouring agent, JECFA number: 959) with many reported beneficial biological effects. The same is true for its ester derivative (methyl vanillate, JECFA number: 159). Based on the increasing evidence that diapocynin, the dimer of apocynin (NADPH oxidase inhibitor), has some improved pharmacological properties compared to its monomer, here the dimer of methyl vanillate (MV), i.e., methyl divanillate (dimer of methyl vanillate, DMV) was synthesized and studied in the context of its redox properties and binding affinity with human serum albumin (HSA). We found that the antioxidant potency of DMV was significantly increased compared to MV. In this regard, the reduction of 2,2-diphenyl-1-picrylhydrazyl (DPPH) free radical by DMV was 30-fold more effective compared to MV. Ferric ion reduction was 4-fold higher and peroxyl radical reduction was 2.7-fold higher. The interaction with HSA was significantly improved (Stern-Vomer constants, 3.8 × 105 mol-1 L and 2.3 × 104 mol-1 L, for DMV and MV, respectively). The complexation between DMV and HSA was also evidenced by induced circular dichroism (ICD) signal generation in the former due to its fixation in the asymmetric protein pocket. Density-functional calculations (TD-DFT) showed that the ICD spectrum was related to a DMV conformation bearing a dihedral angle of approximately -60°. Similar dihedral angles were obtained in the lowest and most populated DMV cluster poses obtained by molecular docking simulations. The computational studies and experimental displacement studies revealed that DMV binds preferentially at site I. In conclusion, besides being a powerful antioxidant, DMV is also a strong ligand of HSA. This is the first study on the chemical and biophysical properties of DMV, a compound with potential beneficial biological effects. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-10-06T17:14:12Z 2019-10-06T17:14:12Z 2019-01-01 |
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/10.1039/c9ra02465d RSC Advances, v. 9, n. 35, p. 19983-19992, 2019. 2046-2069 http://hdl.handle.net/11449/190467 10.1039/c9ra02465d 2-s2.0-85068367817 |
url |
http://dx.doi.org/10.1039/c9ra02465d http://hdl.handle.net/11449/190467 |
identifier_str_mv |
RSC Advances, v. 9, n. 35, p. 19983-19992, 2019. 2046-2069 10.1039/c9ra02465d 2-s2.0-85068367817 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
RSC Advances |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
19983-19992 |
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 |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
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1799965519797813248 |