Abstract
Novel C-5 substituted pyrrolotriazines were optimized for dual EGFR and HER2 protein tyrosine kinase inhibition. The lead compound exhibited promising oral efficacy in both EGFR and HER2 driven human tumor xenograft models. It is hypothesized that its C-5 morpholine side chain binds in the ribose phosphate portion of the ATP binding pocket.
MeSH terms
-
Adenosine Triphosphate / chemistry
-
Animals
-
Caco-2 Cells
-
Chemistry, Pharmaceutical / methods*
-
Drug Design
-
Enzyme Inhibitors / pharmacology
-
ErbB Receptors / antagonists & inhibitors*
-
Humans
-
Inhibitory Concentration 50
-
Mice
-
Neoplasm Transplantation
-
Phosphates / chemistry
-
Pyrroles / chemical synthesis*
-
Pyrroles / pharmacology
-
Receptor, ErbB-2 / antagonists & inhibitors*
-
Ribose / chemistry
-
Triazines / chemical synthesis*
-
Triazines / pharmacology
Substances
-
Enzyme Inhibitors
-
Phosphates
-
Pyrroles
-
Triazines
-
Ribose
-
Adenosine Triphosphate
-
ErbB Receptors
-
Receptor, ErbB-2