Bioactive Secondary Metabolites from Phomopsis sp., an Endophytic Fungus from Senna spectabilis

Chemical investigation of an acetonitrile fraction from the endophytic fungus Phomopsis sp. led to the isolation of the new natural product 2-hydroxy-alternariol (7) together with the known compounds cytochalasins J (1) and H (2), 5'-epialtenuene (3) and the mycotoxins alternariol monomethyl et...

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Detalles Bibliográficos
Autores: Chapla, Vanessa Mara [UNESP], Zeraik, Maria Luiza [UNESP], Ximenes, Valdecir F. [UNESP], Zanardi, Lisineia Maria [UNESP], Lopes, Márcia Nasser [UNESP], Cavalheiro, Alberto José [UNESP], Silva, Dulce Helena Siqueira [UNESP], Young, Maria Claudia M., Fonseca, Luiz Marcos da [UNESP], Bolzani, Vanderlan da Silva [UNESP], Araújo, Angela Regina [UNESP]
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:Brasil
Institución:Universidade Estadual Paulista (UNESP)
Repositorio:Repositório Institucional da UNESP
Idioma:inglés
OAI Identifier:oai:repositorio.unesp.br:11449/113198
Acceso en línea:http://dx.doi.org/10.3390/molecules19056597
http://hdl.handle.net/11449/113198
Access Level:acceso abierto
Palabra clave:secondary metabolites
bioactivities
endophytic fungi
Phomopsis sp.
Senna spectabilis
Descripción
Sumario:Chemical investigation of an acetonitrile fraction from the endophytic fungus Phomopsis sp. led to the isolation of the new natural product 2-hydroxy-alternariol (7) together with the known compounds cytochalasins J (1) and H (2), 5'-epialtenuene (3) and the mycotoxins alternariol monomethyl ether (AME, 4), alternariol (AOH, 5) and cytosporone C (6). The structure of the new compound was elucidated by using 1-D and 2-D NMR (nuclear magnetic resonance) and high resolution mass spectrometry. The cytochalasins J (1) and H (2) and AOH (5) exhibited potent inhibition of the total ROS (reactive oxygen species) produced by stimulated human neutrophils and acted as potent potential anti-inflammatory agents. Moreover, cytochalasin H (2) demonstrated antifungal and acetylcholinesterase enzyme (AChE) inhibition in vitro.