Asterriquinones produced by Aspergillus candidus inhibit binding of the Grb-2 adapter to phosphorylated EGF receptor tyrosine kinase

  • J Antibiot (Tokyo). 1999 Mar;52(3):215-23. doi: 10.7164/antibiotics.52.215.
K A Alvi  1 ,  H Pu ,  M Luche ,  A Rice ,  H App ,  G McMahon ,  H Dare ,  B Margolis
Affiliations
  • 1. Natural Products Chemistry Services, MDS Panlabs, Bothell, WA 98011, USA.
PMID: 10348035 DOI: 10.7164/antibiotics.52.215
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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