Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazard

Detalhes bibliográficos
Autor(a) principal: WEI,Liuyi
Data de Publicação: 2022
Outros Autores: JI,Hongwu, SONG,Wenkui, PENG,Shuo, ZHAN,Suhong, QU,Yushan, CHEN,Ming, ZHANG,Di, LIU,Shucheng
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Food Science and Technology (Campinas)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000100915
Resumo: Abstract Auxis thazard meat was hydrolyzed by alkaline protease. Auxis thazard hydrolysate (ATH) obtained was isolated by ultrafiltration, size exclusion chromatography and reversed-phase high-performance liquid chromatography. Two peptides with high XOD inhibitory activity purified from ATH were identified as Pro-Asp-Leu (PDL, 344.87 Da) and Ser-Val-Gly-Gly-Ala-Leu (SVGGAL, 504.26 Da) by UPLC-MS/MS, which possessed high in vitro XOD inhibitory activity with the IC50 values of 4.37 ± 0.11 mg mL-1 and 5.59 ± 0.09 mg mL-1, respectively. Molecular simulation indicated that PDL and SVGGAL binded to XOD mainly through hydrogen bond and hydrophobic interaction, thereby inhibiting XOD activity. The research results suggested that the two peptides had potential application prospects as a safe XOD inhibitor substance for hyperuricemia treatment.
id SBCTA-1_e200514051674c42f17af5f326bace46
oai_identifier_str oai:scielo:S0101-20612022000100915
network_acronym_str SBCTA-1
network_name_str Food Science and Technology (Campinas)
repository_id_str
spelling Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazardAuxis thazard hydrolysate (ATH)XOD inhibiting peptidesidentificationmolecular dockingAbstract Auxis thazard meat was hydrolyzed by alkaline protease. Auxis thazard hydrolysate (ATH) obtained was isolated by ultrafiltration, size exclusion chromatography and reversed-phase high-performance liquid chromatography. Two peptides with high XOD inhibitory activity purified from ATH were identified as Pro-Asp-Leu (PDL, 344.87 Da) and Ser-Val-Gly-Gly-Ala-Leu (SVGGAL, 504.26 Da) by UPLC-MS/MS, which possessed high in vitro XOD inhibitory activity with the IC50 values of 4.37 ± 0.11 mg mL-1 and 5.59 ± 0.09 mg mL-1, respectively. Molecular simulation indicated that PDL and SVGGAL binded to XOD mainly through hydrogen bond and hydrophobic interaction, thereby inhibiting XOD activity. The research results suggested that the two peptides had potential application prospects as a safe XOD inhibitor substance for hyperuricemia treatment.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2022-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000100915Food Science and Technology v.42 2022reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/fst.106921info:eu-repo/semantics/openAccessWEI,LiuyiJI,HongwuSONG,WenkuiPENG,ShuoZHAN,SuhongQU,YushanCHEN,MingZHANG,DiLIU,Shuchengeng2022-03-15T00:00:00Zoai:scielo:S0101-20612022000100915Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2022-03-15T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false
dc.title.none.fl_str_mv Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazard
title Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazard
spellingShingle Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazard
WEI,Liuyi
Auxis thazard hydrolysate (ATH)
XOD inhibiting peptides
identification
molecular docking
title_short Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazard
title_full Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazard
title_fullStr Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazard
title_full_unstemmed Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazard
title_sort Identification and molecular docking of two novel peptides with xanthine oxidase inhibitory activity from Auxis thazard
author WEI,Liuyi
author_facet WEI,Liuyi
JI,Hongwu
SONG,Wenkui
PENG,Shuo
ZHAN,Suhong
QU,Yushan
CHEN,Ming
ZHANG,Di
LIU,Shucheng
author_role author
author2 JI,Hongwu
SONG,Wenkui
PENG,Shuo
ZHAN,Suhong
QU,Yushan
CHEN,Ming
ZHANG,Di
LIU,Shucheng
author2_role author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv WEI,Liuyi
JI,Hongwu
SONG,Wenkui
PENG,Shuo
ZHAN,Suhong
QU,Yushan
CHEN,Ming
ZHANG,Di
LIU,Shucheng
dc.subject.por.fl_str_mv Auxis thazard hydrolysate (ATH)
XOD inhibiting peptides
identification
molecular docking
topic Auxis thazard hydrolysate (ATH)
XOD inhibiting peptides
identification
molecular docking
description Abstract Auxis thazard meat was hydrolyzed by alkaline protease. Auxis thazard hydrolysate (ATH) obtained was isolated by ultrafiltration, size exclusion chromatography and reversed-phase high-performance liquid chromatography. Two peptides with high XOD inhibitory activity purified from ATH were identified as Pro-Asp-Leu (PDL, 344.87 Da) and Ser-Val-Gly-Gly-Ala-Leu (SVGGAL, 504.26 Da) by UPLC-MS/MS, which possessed high in vitro XOD inhibitory activity with the IC50 values of 4.37 ± 0.11 mg mL-1 and 5.59 ± 0.09 mg mL-1, respectively. Molecular simulation indicated that PDL and SVGGAL binded to XOD mainly through hydrogen bond and hydrophobic interaction, thereby inhibiting XOD activity. The research results suggested that the two peptides had potential application prospects as a safe XOD inhibitor substance for hyperuricemia treatment.
publishDate 2022
dc.date.none.fl_str_mv 2022-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000100915
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000100915
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/fst.106921
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Ciência e Tecnologia de Alimentos
publisher.none.fl_str_mv Sociedade Brasileira de Ciência e Tecnologia de Alimentos
dc.source.none.fl_str_mv Food Science and Technology v.42 2022
reponame:Food Science and Technology (Campinas)
instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
instacron:SBCTA
instname_str Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
instacron_str SBCTA
institution SBCTA
reponame_str Food Science and Technology (Campinas)
collection Food Science and Technology (Campinas)
repository.name.fl_str_mv Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)
repository.mail.fl_str_mv ||revista@sbcta.org.br
_version_ 1752126333618487296

Registros relacionados