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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Authors: 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
Format: article
Status:Published version
Publication Date:2023
Country:España
Institution:Consejo Superior de Investigaciones Científicas (CSIC)
Repository:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/308130
Online Access:http://hdl.handle.net/10261/308130
Access Level:Open access
Keyword: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, 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 Legumes Sweet lupin Vicilin Anti-inflammatory Molecular nutraceutics Redox regulatory capacity Mobile arm structural domain Truncated β-conglutins 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. 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 reviewed Multidisciplinary Digital Publishing Institute http://hdl.handle.net/10261/308130
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.)
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
topic Legumes
Sweet lupin
Vicilin
Anti-inflammatory
Molecular nutraceutics
Redox regulatory capacity
Mobile arm structural domain
Truncated β-conglutins
topic_facet 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
format article
status_str publishedVersion
url http://hdl.handle.net/10261/308130
eu_rights_str_mv openAccess
publisher Multidisciplinary Digital Publishing Institute
institution Consejo Superior de Investigaciones Científicas (CSIC)
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
_version_ 1878439488282165248
publishDateSort 2023
author_browse Escudero-Feliú, Julia
García-Fernandez, Pedro
Jiménez-López, José Carlos
León, Josefa
Lima Cabello, Elena
Núñez, María Isabel
Peralta, Andreína
Siddique, Kadambot H. M.
Singh, Karam B.
publisherStr Multidisciplinary Digital Publishing Institute
score 6.9303427