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