ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E V

Detalhes bibliográficos
Autor(a) principal: Marques,Emerson F.
Data de Publicação: 2016
Outros Autores: Vieira,Paulo C., Severino,Richele P.
Tipo de documento: Artigo
Idioma: por
Título da fonte: Química Nova (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422016000100058
Resumo: Cathepsins represent a class of enzymes that has the primary function of randomly degrading proteins in the lysosomes, although are also involved in different pathologies. The aim of this paper was to evaluate the capacity of acridone alkaloids isolated from Swinglea glutinosa (Rutaceae) to inhibit cathepsin L in vitro . The IC50 values found were in the 0.8-57 µM range and the most promising compounds were alkaloids 1 and 2, with IC50 of 0.9 and 0.8 µM, respectively. Enzyme kinetics revealed that they are reversible competitive inhibitors with respect to the substrate Z-FR-MCA. This small series of acridone alkaloids showed low selectivity for both cathepsins, but represent promising lead candidates for the further development of competitive cathepsin L and V inhibitors.
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spelling ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E Vcathepsin Linhibitorsnatural productsacridone alkaloidsCathepsins represent a class of enzymes that has the primary function of randomly degrading proteins in the lysosomes, although are also involved in different pathologies. The aim of this paper was to evaluate the capacity of acridone alkaloids isolated from Swinglea glutinosa (Rutaceae) to inhibit cathepsin L in vitro . The IC50 values found were in the 0.8-57 µM range and the most promising compounds were alkaloids 1 and 2, with IC50 of 0.9 and 0.8 µM, respectively. Enzyme kinetics revealed that they are reversible competitive inhibitors with respect to the substrate Z-FR-MCA. This small series of acridone alkaloids showed low selectivity for both cathepsins, but represent promising lead candidates for the further development of competitive cathepsin L and V inhibitors.Sociedade Brasileira de Química2016-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422016000100058Química Nova v.39 n.1 2016reponame:Química Nova (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.5935/0100-4042.20150176info:eu-repo/semantics/openAccessMarques,Emerson F.Vieira,Paulo C.Severino,Richele P.por2016-02-29T00:00:00Zoai:scielo:S0100-40422016000100058Revistahttps://www.scielo.br/j/qn/ONGhttps://old.scielo.br/oai/scielo-oai.phpquimicanova@sbq.org.br1678-70640100-4042opendoar:2016-02-29T00:00Química Nova (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E V
title ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E V
spellingShingle ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E V
Marques,Emerson F.
cathepsin L
inhibitors
natural products
acridone alkaloids
title_short ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E V
title_full ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E V
title_fullStr ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E V
title_full_unstemmed ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E V
title_sort ALCALOIDES ACRIDÔNICOS INIBEM CATEPSINA L E V
author Marques,Emerson F.
author_facet Marques,Emerson F.
Vieira,Paulo C.
Severino,Richele P.
author_role author
author2 Vieira,Paulo C.
Severino,Richele P.
author2_role author
author
dc.contributor.author.fl_str_mv Marques,Emerson F.
Vieira,Paulo C.
Severino,Richele P.
dc.subject.por.fl_str_mv cathepsin L
inhibitors
natural products
acridone alkaloids
topic cathepsin L
inhibitors
natural products
acridone alkaloids
description Cathepsins represent a class of enzymes that has the primary function of randomly degrading proteins in the lysosomes, although are also involved in different pathologies. The aim of this paper was to evaluate the capacity of acridone alkaloids isolated from Swinglea glutinosa (Rutaceae) to inhibit cathepsin L in vitro . The IC50 values found were in the 0.8-57 µM range and the most promising compounds were alkaloids 1 and 2, with IC50 of 0.9 and 0.8 µM, respectively. Enzyme kinetics revealed that they are reversible competitive inhibitors with respect to the substrate Z-FR-MCA. This small series of acridone alkaloids showed low selectivity for both cathepsins, but represent promising lead candidates for the further development of competitive cathepsin L and V inhibitors.
publishDate 2016
dc.date.none.fl_str_mv 2016-01-01
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=S0100-40422016000100058
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422016000100058
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv 10.5935/0100-4042.20150176
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 Química
publisher.none.fl_str_mv Sociedade Brasileira de Química
dc.source.none.fl_str_mv Química Nova v.39 n.1 2016
reponame:Química Nova (Online)
instname:Sociedade Brasileira de Química (SBQ)
instacron:SBQ
instname_str Sociedade Brasileira de Química (SBQ)
instacron_str SBQ
institution SBQ
reponame_str Química Nova (Online)
collection Química Nova (Online)
repository.name.fl_str_mv Química Nova (Online) - Sociedade Brasileira de Química (SBQ)
repository.mail.fl_str_mv quimicanova@sbq.org.br
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