Abstract
A set of novel fragment-like catechol derivatives were identified as EphA2 inhibitors and were further profiled against a panel of 19 tyrosine kinases. In addition to EphA2, the recovered hits were active against EGFR, FGFR1, FGFR2, Abl and PDGFR-a, and according to molecular modelling studies catechol moiety was capable of forming two or more correlated hydrogen bonds with the kinase hinge region, suggesting prospects of its further optimization as an EphA2 inhibitor.
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