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During the past decade, the basophilic atypical kinase Haspin has emerged as a key player in mitosis responsible for phosphorylation of Thr3 residue of histone H3. Here, we report the construction of conjugates comprising an aromatic fragment targeted to the ATP-site of Haspin and a peptide mimicking the N-terminus of histone H3. The combination of effective solid phase synthesis procedures and a high throughput binding/displacement assay with fluorescence anisotropy readout afforded the development of inhibitors with remarkable subnanomolar affinity toward Haspin. The selectivity profiles of novel conjugates were established by affinity studies with a model basophilic kinase (catalytic subunit of cAMP-dependent protein kinase) and by a commercial 1-point inhibition assay with 43 protein kinases.

Original publication

DOI

10.1021/bc500464r

Type

Journal article

Journal

Bioconjug Chem

Publication Date

18/02/2015

Volume

26

Pages

225 - 234

Keywords

Adenosine Triphosphate, Amino Acid Sequence, Binding Sites, Histones, Humans, Intracellular Signaling Peptides and Proteins, Mitosis, Models, Molecular, Peptides, Protein Kinase Inhibitors, Protein-Serine-Threonine Kinases, Recombinant Proteins