Beta conglutins’ unique mobile arm Is a key structural domain involved in molecular nutraceutical properties of narrow-leafed Lupin (Lupinus angustifolius L.)

Narrow-leafed lupin (NLL; Lupinus angustifolius L.) has multiple nutraceutical properties that may result from unique structural features of β-conglutin proteins, such as the mobile arm at the N-terminal, a structural domain rich in α-helices. A similar domain has not been found in other vicilin pro...

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Autores: Lima Cabello, Elena, Escudero-Feliú, Julia, Peralta, Andreína, García-Fernandez, Pedro, Siddique, Kadambot H. M., Singh, Karam B., Núñez, María Isabel, León, Josefa, Jiménez-López, José Carlos
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/308130
Acceso en línea:http://hdl.handle.net/10261/308130
Access Level:acceso abierto
Palabra clave:Legumes
Sweet lupin
Vicilin
Anti-inflammatory
Molecular nutraceutics
Redox regulatory capacity
Mobile arm structural domain
Truncated β-conglutins
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spelling Beta conglutins’ unique mobile arm Is a key structural domain involved in molecular nutraceutical properties of narrow-leafed Lupin (Lupinus angustifolius L.)Lima Cabello, ElenaEscudero-Feliú, JuliaPeralta, AndreínaGarcía-Fernandez, PedroSiddique, Kadambot H. M.Singh, Karam B.Núñez, María IsabelLeón, JosefaJiménez-López, José CarlosLegumesSweet lupinVicilinAnti-inflammatoryMolecular nutraceuticsRedox regulatory capacityMobile arm structural domainTruncated β-conglutinsNarrow-leafed lupin (NLL; Lupinus angustifolius L.) has multiple nutraceutical properties that may result from unique structural features of β-conglutin proteins, such as the mobile arm at the N-terminal, a structural domain rich in α-helices. A similar domain has not been found in other vicilin proteins of legume species. We used affinity chromatography to purify recombinant complete and truncated (without the mobile arm domain, tβ5 and tβ7) forms of NLL β5 and β7 conglutin proteins. We then used biochemical and molecular biology techniques in ex vivo and in vitro systems to evaluate their anti-inflammatory activity and antioxidant capacity. The complete β5 and β7 conglutin proteins decreased pro-inflammatory mediator levels (e.g., nitric oxide), mRNA expression levels (iNOS, TNFα, IL-1β), and the protein levels of pro-inflammatory cytokine TNF-α, interleukins (IL-1β, IL-2, IL-6, IL-8, IL-12, IL-17, IL-27), and other mediators (INFγ, MOP, S-TNF-R1/-R2, and TWEAK), and exerted a regulatory oxidative balance effect in cells as demonstrated in glutathione, catalase, and superoxide dismutase assays. The truncated tβ5 and tβ7 conglutin proteins did not have these molecular effects. These results suggest that β5 and β7 conglutins have potential as functional food components due to their anti-inflammatory and oxidative cell state regulatory properties, and that the mobile arm of NLL β-conglutin proteins is a key domain in the development of nutraceutical properties, making NLL β5 and β7 excellent innovative candidates as functional foods.This study was funded by the European Research Program MARIE CURIE (FP7-PEOPLE-2011-IOF), grant ref. PIOF-GA-2011-301550; the Spanish Ministry of Economy, Industry and Competitiveness (Ramon y Cajal Research Program), grant ref. RYC-2014-16536; the CSIC intramural research program, grant ref. 202240I002; the Spanish Ministry of Science and Innovation, grant ref. number CPP2021-008989.Peer reviewedMultidisciplinary Digital Publishing InstituteEuropean CommissionMinisterio de Economía y Competitividad (España)Consejo Superior de Investigaciones Científicas (España)Ministerio de Ciencia e Innovación (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2023202320232023info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/308130reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/EC/FP7/301550info:eu-repo/grantAgreement/MINECO//RYC-2014-16536info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/CPP2021-008989https://doi.org/10.3390/ijms24087676Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3081302026-05-22T06:33:51Z
dc.title.none.fl_str_mv Beta conglutins’ unique mobile arm Is a key structural domain involved in molecular nutraceutical properties of narrow-leafed Lupin (Lupinus angustifolius L.)
title Beta conglutins’ unique mobile arm Is a key structural domain involved in molecular nutraceutical properties of narrow-leafed Lupin (Lupinus angustifolius L.)
spellingShingle Beta conglutins’ unique mobile arm Is a key structural domain involved in molecular nutraceutical properties of narrow-leafed Lupin (Lupinus angustifolius L.)
Lima Cabello, Elena
Legumes
Sweet lupin
Vicilin
Anti-inflammatory
Molecular nutraceutics
Redox regulatory capacity
Mobile arm structural domain
Truncated β-conglutins
title_short Beta conglutins’ unique mobile arm Is a key structural domain involved in molecular nutraceutical properties of narrow-leafed Lupin (Lupinus angustifolius L.)
title_full Beta conglutins’ unique mobile arm Is a key structural domain involved in molecular nutraceutical properties of narrow-leafed Lupin (Lupinus angustifolius L.)
title_fullStr Beta conglutins’ unique mobile arm Is a key structural domain involved in molecular nutraceutical properties of narrow-leafed Lupin (Lupinus angustifolius L.)
title_full_unstemmed Beta conglutins’ unique mobile arm Is a key structural domain involved in molecular nutraceutical properties of narrow-leafed Lupin (Lupinus angustifolius L.)
title_sort Beta conglutins’ unique mobile arm Is a key structural domain involved in molecular nutraceutical properties of narrow-leafed Lupin (Lupinus angustifolius L.)
dc.creator.none.fl_str_mv Lima Cabello, Elena
Escudero-Feliú, Julia
Peralta, Andreína
García-Fernandez, Pedro
Siddique, Kadambot H. M.
Singh, Karam B.
Núñez, María Isabel
León, Josefa
Jiménez-López, José Carlos
author Lima Cabello, Elena
author_facet Lima Cabello, Elena
Escudero-Feliú, Julia
Peralta, Andreína
García-Fernandez, Pedro
Siddique, Kadambot H. M.
Singh, Karam B.
Núñez, María Isabel
León, Josefa
Jiménez-López, José Carlos
author_role author
author2 Escudero-Feliú, Julia
Peralta, Andreína
García-Fernandez, Pedro
Siddique, Kadambot H. M.
Singh, Karam B.
Núñez, María Isabel
León, Josefa
Jiménez-López, José Carlos
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv European Commission
Ministerio de Economía y Competitividad (España)
Consejo Superior de Investigaciones Científicas (España)
Ministerio de Ciencia e Innovación (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Legumes
Sweet lupin
Vicilin
Anti-inflammatory
Molecular nutraceutics
Redox regulatory capacity
Mobile arm structural domain
Truncated β-conglutins
topic Legumes
Sweet lupin
Vicilin
Anti-inflammatory
Molecular nutraceutics
Redox regulatory capacity
Mobile arm structural domain
Truncated β-conglutins
description Narrow-leafed lupin (NLL; Lupinus angustifolius L.) has multiple nutraceutical properties that may result from unique structural features of β-conglutin proteins, such as the mobile arm at the N-terminal, a structural domain rich in α-helices. A similar domain has not been found in other vicilin proteins of legume species. We used affinity chromatography to purify recombinant complete and truncated (without the mobile arm domain, tβ5 and tβ7) forms of NLL β5 and β7 conglutin proteins. We then used biochemical and molecular biology techniques in ex vivo and in vitro systems to evaluate their anti-inflammatory activity and antioxidant capacity. The complete β5 and β7 conglutin proteins decreased pro-inflammatory mediator levels (e.g., nitric oxide), mRNA expression levels (iNOS, TNFα, IL-1β), and the protein levels of pro-inflammatory cytokine TNF-α, interleukins (IL-1β, IL-2, IL-6, IL-8, IL-12, IL-17, IL-27), and other mediators (INFγ, MOP, S-TNF-R1/-R2, and TWEAK), and exerted a regulatory oxidative balance effect in cells as demonstrated in glutathione, catalase, and superoxide dismutase assays. The truncated tβ5 and tβ7 conglutin proteins did not have these molecular effects. These results suggest that β5 and β7 conglutins have potential as functional food components due to their anti-inflammatory and oxidative cell state regulatory properties, and that the mobile arm of NLL β-conglutin proteins is a key domain in the development of nutraceutical properties, making NLL β5 and β7 excellent innovative candidates as functional foods.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2023
2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/308130
url http://hdl.handle.net/10261/308130
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
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#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/EC/FP7/301550
info:eu-repo/grantAgreement/MINECO//RYC-2014-16536
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/CPP2021-008989
https://doi.org/10.3390/ijms24087676
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
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