Pyrimidine-based inhibitors of CaMKIIδ

Non-ATP competitive pyrimidine-based inhibitors of CaMKIIδ were identified. Computational studies were enlisted to predict the probable mode of binding. The results of the computational studies led to the design of ATP competitive inhibitors with optimized hinge interactions. Inhibitors of this class possessed improved enzyme and cellular activity compared to early leads.

Pyrimidine-based inhibitors of CaMKIIδ were identified. Through computational studies, a probable binding mode was identified leading to the design of ATP competitive inhibitors with improved potency, potential hinge interactions, and potent cellular activity.Figure optionsDownload as PowerPoint slide