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Selective inhibitors of DYRK1A are of interest for the treatment of cancer, Type 2 diabetes and neurological disorders. Optimization of imidazo [1,2-b]pyridazine fragment 1 through structure-activity relationship exploration and in silico drug design efforts led to the discovery of compound 17 as a potent cellular inhibitor of DYRK1A with selectivity over much of the kinome. The binding mode of compound 17 was elucidated with X-ray crystallography, facilitating the rational design of compound 29, an imidazo [1,2-b]pyridazine with improved kinase selectivity with respect to closely related CLK kinases.

Original publication

DOI

10.1016/j.ejmech.2024.116292

Type

Journal article

Journal

European journal of medicinal chemistry

Publication Date

03/2024

Volume

269

Addresses

Sussex Drug Discovery Centre, University of Sussex, Brighton, BN1 9RH, UK. Electronic address: scott.henderson@benevolent.ai.