Inhibition of cysteine proteases by a natural biflavone : behavioral evaluation of fukugetin as papain and cruzain inhibitor.

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.creatorAssis, Diego Magno-
Autor(es): dc.creatorGontijo, Vanessa Silva-
Autor(es): dc.creatorPereira, Ivan de Oliveira-
Autor(es): dc.creatorSantos, Jorge Alexandre Nogueira-
Autor(es): dc.creatorCamps, Ihosvany-
Autor(es): dc.creatorNagem, Tanus Jorge-
Autor(es): dc.creatorIzidoro, Mario Augusto-
Autor(es): dc.creatorTersariol, Ivarne Luis dos Santos-
Autor(es): dc.creatorBarros, Nilana Meza Tenório de-
Autor(es): dc.creatorDoriguetto, Antônio Carlos-
Autor(es): dc.creatorSantos, Marcelo Henrique dos-
Autor(es): dc.creatorJuliano, Maria Aparecida-
Data de aceite: dc.date.accessioned2025-08-21T15:12:43Z-
Data de disponibilização: dc.date.available2025-08-21T15:12:43Z-
Data de envio: dc.date.issued2017-06-13-
Data de envio: dc.date.issued2017-06-13-
Data de envio: dc.date.issued2012-
Fonte completa do material: dc.identifierhttp://www.repositorio.ufop.br/handle/123456789/7943-
Fonte completa do material: dc.identifierhttp://www.tandfonline.com/doi/full/10.3109/14756366.2012.668539-
Fonte completa do material: dc.identifierhttps://doi.org/10.3109/14756366.2012.668539-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1006082-
Descrição: dc.descriptionCruzain is the major cysteine protease of Trypanosoma cruzi, the infectious agent responsible for Chagas disease, and cruzain inhibitors display considerable antitrypanosomal activity. In the present work we elucidated crystallographic data of fukugetin, a biflavone isolated from Garcinia brasiliensis, and investigated the role of this molecule as cysteine protease inhibitor. The kinetic analyses demonstrated that fukugetin inhibited cruzain and papain by a slow reversible type inhibition with KI of 1.1 and 13.4 μM, respectively. However, cruzain inhibition was about 12 times faster than papain inhibition. Lineweaver–Burk plots demonstrated partial competitive inhibition for cruzain and hyperbolic mixed-type inhibition for papain. Furthermore, the docking results showed that the biflavone binds to ring C′ in the S2 pocket and to ring C in the S3 pocket through hydrophobic interactions and hydrogen bonds. Finally, fukugetin also presented inhibitory activity on proteases of the T. cruzi extract, with IC50 of 7 μM.-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Direitos: dc.rightsrestrito-
Palavras-chave: dc.subjectBiflavones-
Palavras-chave: dc.subjectProtease inhibition-
Palavras-chave: dc.subjectMolecular docking-
Palavras-chave: dc.subjectCysteine proteases-
Título: dc.titleInhibition of cysteine proteases by a natural biflavone : behavioral evaluation of fukugetin as papain and cruzain inhibitor.-
Aparece nas coleções:Repositório Institucional - UFOP

Não existem arquivos associados a este item.