Mechanism of inhibition of α-glucosidase activity by bavachalcone

Detalhes bibliográficos
Autor(a) principal: FENG,Yingying
Data de Publicação: 2022
Outros Autores: NAN,Haijuan, ZHOU,Haoyu, XI,Penghang, LI,Bo
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=S0101-20612022000101008
Resumo: Abstract Bavachalcone is an important active component of the traditional Chinese medicine Fructus Psoraleae. The inhibitory effect of bavachalcone on α-glucosidase activity is reported for the first time and the mechanism elucidated by molecular docking. The inhibition of α-glucosidase by bavachalcone (IC50 15.35 ± 0.57 μg/mL) was significantly superior to acarbose (IC50 2.77 ± 0.09 mg/mL). Inhibition type was mixed competitive and non-competitive. Molecular docking suggested this inhibition stems from hydrogen bonds formed with the trp391, arg428, and trp710 residues of α-glucosidase.
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spelling Mechanism of inhibition of α-glucosidase activity by bavachalconebavachalconeα-glucosidaseinhibition mechanismfluorescence spectroscopymolecular dockingAbstract Bavachalcone is an important active component of the traditional Chinese medicine Fructus Psoraleae. The inhibitory effect of bavachalcone on α-glucosidase activity is reported for the first time and the mechanism elucidated by molecular docking. The inhibition of α-glucosidase by bavachalcone (IC50 15.35 ± 0.57 μg/mL) was significantly superior to acarbose (IC50 2.77 ± 0.09 mg/mL). Inhibition type was mixed competitive and non-competitive. Molecular docking suggested this inhibition stems from hydrogen bonds formed with the trp391, arg428, and trp710 residues of α-glucosidase.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=S0101-20612022000101008Food 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.123421info:eu-repo/semantics/openAccessFENG,YingyingNAN,HaijuanZHOU,HaoyuXI,PenghangLI,Boeng2022-03-15T00:00:00Zoai:scielo:S0101-20612022000101008Revistahttp://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 Mechanism of inhibition of α-glucosidase activity by bavachalcone
title Mechanism of inhibition of α-glucosidase activity by bavachalcone
spellingShingle Mechanism of inhibition of α-glucosidase activity by bavachalcone
FENG,Yingying
bavachalcone
α-glucosidase
inhibition mechanism
fluorescence spectroscopy
molecular docking
title_short Mechanism of inhibition of α-glucosidase activity by bavachalcone
title_full Mechanism of inhibition of α-glucosidase activity by bavachalcone
title_fullStr Mechanism of inhibition of α-glucosidase activity by bavachalcone
title_full_unstemmed Mechanism of inhibition of α-glucosidase activity by bavachalcone
title_sort Mechanism of inhibition of α-glucosidase activity by bavachalcone
author FENG,Yingying
author_facet FENG,Yingying
NAN,Haijuan
ZHOU,Haoyu
XI,Penghang
LI,Bo
author_role author
author2 NAN,Haijuan
ZHOU,Haoyu
XI,Penghang
LI,Bo
author2_role author
author
author
author
dc.contributor.author.fl_str_mv FENG,Yingying
NAN,Haijuan
ZHOU,Haoyu
XI,Penghang
LI,Bo
dc.subject.por.fl_str_mv bavachalcone
α-glucosidase
inhibition mechanism
fluorescence spectroscopy
molecular docking
topic bavachalcone
α-glucosidase
inhibition mechanism
fluorescence spectroscopy
molecular docking
description Abstract Bavachalcone is an important active component of the traditional Chinese medicine Fructus Psoraleae. The inhibitory effect of bavachalcone on α-glucosidase activity is reported for the first time and the mechanism elucidated by molecular docking. The inhibition of α-glucosidase by bavachalcone (IC50 15.35 ± 0.57 μg/mL) was significantly superior to acarbose (IC50 2.77 ± 0.09 mg/mL). Inhibition type was mixed competitive and non-competitive. Molecular docking suggested this inhibition stems from hydrogen bonds formed with the trp391, arg428, and trp710 residues of α-glucosidase.
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=S0101-20612022000101008
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101008
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/fst.123421
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
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