Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies

Autores
Santi, María Daniela; Bedoya Aguirre, Einy Nallybe; Negro, Melisa Fabiana; Zunini, M. Paulino; Peralta, Mariana Andrea; Ortega, María Gabriela
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Prenylated flavanones are a family of compounds with an important biological potential. Previously, anti-tyrosinase activity, acetylcholinesterase inhibitory activity, and neuroprotective effects of several prenyl flavanones isolated from different American Dalea genus species were reported. The biological potency of these kinds of compounds, together with the particularity of their chemical structures, encouraged us to investigate them for in vitro and in silico anti-xanthine oxidase activity. So, five prenyl-flavanones obtained from different Dalea sp (Dalea elegans, Dalea boliviana, and Dalea pazensis) were studied and the relationships between the structure of these prenyl-flavanones and their inhibitory activity were evaluated. Molecular docking studies were performed in order to propose the binding mode of the most active natural compound. 2′,4′-dihydroxy-5′-(1‴,1‴-dimethylallyl)-8-prenylpinocembrin (1) was the most active in this series showing an IC50 of 0.26 ± 0.07 µM comparable with the reference inhibitor, allopurinol. The presence of 5,7,2′,4′-tetrahydroxy substitution, accompanied by a prenyl group at 8-position in the A-ring, and a 5′ (1‴,1‴-dimethylallyl) were important to present a xanthine oxidase inhibitory activity. This fact was confirmed with molecular docking studies showing relevant interactions of 1 with the residues of the catalytic site of xanthine oxidase, and a binding energy of −7.3297 kcal mol−1. These results contributed not only to understanding the binding mode but also to validating the in vitro results. The obtained findings lead us to propose these prenyl-flavanones as lead compounds for the design and development of novel xanthine oxidase inhibitors for the treatment of diseases in which this enzyme is involved.
Fil: Santi, María Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Fil: Bedoya Aguirre, Einy Nallybe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Fil: Negro, Melisa Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Fil: Zunini, M. Paulino. Universidad de la República; Uruguay
Fil: Peralta, Mariana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Fil: Ortega, María Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Materia
DALEA GENUS
GOUT
HYPERURICEMIA
MOLECULAR DOCKING
PRENYLATED FLAVANONES
XANTHINE OXIDASE INHIBITION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/220483
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/220483
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studiesSanti, María DanielaBedoya Aguirre, Einy NallybeNegro, Melisa FabianaZunini, M. PaulinoPeralta, Mariana AndreaOrtega, María GabrielaDALEA GENUSGOUTHYPERURICEMIAMOLECULAR DOCKINGPRENYLATED FLAVANONESXANTHINE OXIDASE INHIBITIONhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Prenylated flavanones are a family of compounds with an important biological potential. Previously, anti-tyrosinase activity, acetylcholinesterase inhibitory activity, and neuroprotective effects of several prenyl flavanones isolated from different American Dalea genus species were reported. The biological potency of these kinds of compounds, together with the particularity of their chemical structures, encouraged us to investigate them for in vitro and in silico anti-xanthine oxidase activity. So, five prenyl-flavanones obtained from different Dalea sp (Dalea elegans, Dalea boliviana, and Dalea pazensis) were studied and the relationships between the structure of these prenyl-flavanones and their inhibitory activity were evaluated. Molecular docking studies were performed in order to propose the binding mode of the most active natural compound. 2′,4′-dihydroxy-5′-(1‴,1‴-dimethylallyl)-8-prenylpinocembrin (1) was the most active in this series showing an IC50 of 0.26 ± 0.07 µM comparable with the reference inhibitor, allopurinol. The presence of 5,7,2′,4′-tetrahydroxy substitution, accompanied by a prenyl group at 8-position in the A-ring, and a 5′ (1‴,1‴-dimethylallyl) were important to present a xanthine oxidase inhibitory activity. This fact was confirmed with molecular docking studies showing relevant interactions of 1 with the residues of the catalytic site of xanthine oxidase, and a binding energy of −7.3297 kcal mol−1. These results contributed not only to understanding the binding mode but also to validating the in vitro results. The obtained findings lead us to propose these prenyl-flavanones as lead compounds for the design and development of novel xanthine oxidase inhibitors for the treatment of diseases in which this enzyme is involved.Fil: Santi, María Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; ArgentinaFil: Bedoya Aguirre, Einy Nallybe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; ArgentinaFil: Negro, Melisa Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; ArgentinaFil: Zunini, M. Paulino. Universidad de la República; UruguayFil: Peralta, Mariana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; ArgentinaFil: Ortega, María Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; ArgentinaElsevier2023-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/220483Santi, María Daniela; Bedoya Aguirre, Einy Nallybe; Negro, Melisa Fabiana; Zunini, M. Paulino; Peralta, Mariana Andrea; et al.; Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies; Elsevier; Results in Chemistry; 6; 12-2023; 1-72211-7156CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.rechem.2023.101115info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S2211715623003545info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:08:28Zoai:ri.conicet.gov.ar:11336/220483instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:08:28.633CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies
title Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies
spellingShingle Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies
Santi, María Daniela
DALEA GENUS
GOUT
HYPERURICEMIA
MOLECULAR DOCKING
PRENYLATED FLAVANONES
XANTHINE OXIDASE INHIBITION
title_short Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies
title_full Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies
title_fullStr Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies
title_full_unstemmed Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies
title_sort Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies
dc.creator.none.fl_str_mv Santi, María Daniela
Bedoya Aguirre, Einy Nallybe
Negro, Melisa Fabiana
Zunini, M. Paulino
Peralta, Mariana Andrea
Ortega, María Gabriela
author Santi, María Daniela
author_facet Santi, María Daniela
Bedoya Aguirre, Einy Nallybe
Negro, Melisa Fabiana
Zunini, M. Paulino
Peralta, Mariana Andrea
Ortega, María Gabriela
author_role author
author2 Bedoya Aguirre, Einy Nallybe
Negro, Melisa Fabiana
Zunini, M. Paulino
Peralta, Mariana Andrea
Ortega, María Gabriela
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv DALEA GENUS
GOUT
HYPERURICEMIA
MOLECULAR DOCKING
PRENYLATED FLAVANONES
XANTHINE OXIDASE INHIBITION
topic DALEA GENUS
GOUT
HYPERURICEMIA
MOLECULAR DOCKING
PRENYLATED FLAVANONES
XANTHINE OXIDASE INHIBITION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Prenylated flavanones are a family of compounds with an important biological potential. Previously, anti-tyrosinase activity, acetylcholinesterase inhibitory activity, and neuroprotective effects of several prenyl flavanones isolated from different American Dalea genus species were reported. The biological potency of these kinds of compounds, together with the particularity of their chemical structures, encouraged us to investigate them for in vitro and in silico anti-xanthine oxidase activity. So, five prenyl-flavanones obtained from different Dalea sp (Dalea elegans, Dalea boliviana, and Dalea pazensis) were studied and the relationships between the structure of these prenyl-flavanones and their inhibitory activity were evaluated. Molecular docking studies were performed in order to propose the binding mode of the most active natural compound. 2′,4′-dihydroxy-5′-(1‴,1‴-dimethylallyl)-8-prenylpinocembrin (1) was the most active in this series showing an IC50 of 0.26 ± 0.07 µM comparable with the reference inhibitor, allopurinol. The presence of 5,7,2′,4′-tetrahydroxy substitution, accompanied by a prenyl group at 8-position in the A-ring, and a 5′ (1‴,1‴-dimethylallyl) were important to present a xanthine oxidase inhibitory activity. This fact was confirmed with molecular docking studies showing relevant interactions of 1 with the residues of the catalytic site of xanthine oxidase, and a binding energy of −7.3297 kcal mol−1. These results contributed not only to understanding the binding mode but also to validating the in vitro results. The obtained findings lead us to propose these prenyl-flavanones as lead compounds for the design and development of novel xanthine oxidase inhibitors for the treatment of diseases in which this enzyme is involved.
Fil: Santi, María Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Fil: Bedoya Aguirre, Einy Nallybe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Fil: Negro, Melisa Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Fil: Zunini, M. Paulino. Universidad de la República; Uruguay
Fil: Peralta, Mariana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Fil: Ortega, María Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
description Prenylated flavanones are a family of compounds with an important biological potential. Previously, anti-tyrosinase activity, acetylcholinesterase inhibitory activity, and neuroprotective effects of several prenyl flavanones isolated from different American Dalea genus species were reported. The biological potency of these kinds of compounds, together with the particularity of their chemical structures, encouraged us to investigate them for in vitro and in silico anti-xanthine oxidase activity. So, five prenyl-flavanones obtained from different Dalea sp (Dalea elegans, Dalea boliviana, and Dalea pazensis) were studied and the relationships between the structure of these prenyl-flavanones and their inhibitory activity were evaluated. Molecular docking studies were performed in order to propose the binding mode of the most active natural compound. 2′,4′-dihydroxy-5′-(1‴,1‴-dimethylallyl)-8-prenylpinocembrin (1) was the most active in this series showing an IC50 of 0.26 ± 0.07 µM comparable with the reference inhibitor, allopurinol. The presence of 5,7,2′,4′-tetrahydroxy substitution, accompanied by a prenyl group at 8-position in the A-ring, and a 5′ (1‴,1‴-dimethylallyl) were important to present a xanthine oxidase inhibitory activity. This fact was confirmed with molecular docking studies showing relevant interactions of 1 with the residues of the catalytic site of xanthine oxidase, and a binding energy of −7.3297 kcal mol−1. These results contributed not only to understanding the binding mode but also to validating the in vitro results. The obtained findings lead us to propose these prenyl-flavanones as lead compounds for the design and development of novel xanthine oxidase inhibitors for the treatment of diseases in which this enzyme is involved.
publishDate 2023
dc.date.none.fl_str_mv 2023-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/220483
Santi, María Daniela; Bedoya Aguirre, Einy Nallybe; Negro, Melisa Fabiana; Zunini, M. Paulino; Peralta, Mariana Andrea; et al.; Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies; Elsevier; Results in Chemistry; 6; 12-2023; 1-7
2211-7156
CONICET Digital
CONICET
url http://hdl.handle.net/11336/220483
identifier_str_mv Santi, María Daniela; Bedoya Aguirre, Einy Nallybe; Negro, Melisa Fabiana; Zunini, M. Paulino; Peralta, Mariana Andrea; et al.; Prenylated flavonoids from Dalea genus as xanthine oxidase inhibitors: In vitro bioactivity evaluation and molecular docking studies; Elsevier; Results in Chemistry; 6; 12-2023; 1-7
2211-7156
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.rechem.2023.101115
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S2211715623003545
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
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instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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