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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
