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...
| Authors: | , , , , , , , , |
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| 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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oai:digital.csic.es:10261/308130 |
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España |
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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 |