Asterriquinones produced by Aspergillus candidus inhibit binding of the Grb-2 adapter to phosphorylated EGF receptor tyrosine kinase.
J Antibiot (Tokyo)
; 52(3): 215-23, 1999 Mar.
Article
em En
| MEDLINE
| ID: mdl-10348035
ABSTRACT
Five new asterriquinone analogs (2-4, 6, 7), together with previously identified neoasterriquinone (1) and isoasterriquinone (5), were isolated from a fermentation broth of the fungus Aspergillus candidus and purified by HSCCC (high speed counter current chromatography) followed by HPLC. The structures were determined by 1D and 2D NMR and MS/MS techniques. All seven showed inhibitory activity against the binding of a recombinant protein containing the SH2 protein domain of Grb-2 to the tyrosine phosphorylated form of the EGF receptor tyrosine kinase. Some of these asterriquinones exhibited specific inhibition of Grb-2 binding compared to Grb-7 and PLC-gamma.
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Base de dados:
MEDLINE
Assunto principal:
Aspergillus
/
Proteínas de Transporte
/
Proteínas Adaptadoras de Transdução de Sinal
/
Receptores ErbB
/
Antibióticos Antineoplásicos
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
1999
Tipo de documento:
Article