Selective inhibitors of the protein tyrosine phosphatase SHP2 block cellular motility and growth of cancer cells in vitro and in vivo.

Selective inhibitors of the protein tyrosine phosphatase SHP2 (src homology region 2 domain phosphatase; PTPN11), an enzyme that is deregulated in numerous human tumors, were generated through a combination of chemical synthesis and structure-based rational design. Seventy pyridazolon-4-ylidenehydrazinyl benzenesulfonates were prepared and evaluated in enzyme assays. The binding modes of active inhibitors were simulated in silico using a newly generated crystal structure of SHP2.

Comparative action of cobalt carbonyl complexes on cancer cells using human tumor xenografts.

We have previously shown that alkyne-cobalt carbonyl complexes inhibit the growth of human cancer cells. They were more active than dicobalt octacarbonyl, cobalt chloride or the free ligands. A difference in growth inhibition was observed among several cobalt complexes in two different cell lines indicating that the ligand may influence the activity of the complex.