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ID: ALA1149203

Journal: Bioorg Med Chem Lett

Title: Design, synthesis, and characterization of an ATP-peptide conjugate inhibitor of protein kinase A.

Authors: Hines AC, Cole PA.

Abstract: An ATP-peptide conjugate was synthesized as a bisubstrate analogue inhibitor of the serine/threonine kinase protein kinase A. The compound was found to be a linear, competitive inhibitor with respect to ATP substrate, exhibiting a Ki of 3.8 microM. The compound was noncompetitive with respect to peptide substrate. The inhibitor was shown to be selective for protein kinase A versus the closely related protein kinase C as well as tyrosine kinase Csk. This analysis provides new evidence for the dissociative transition state of protein serine/threonine kinases and illustrates a simple method to convert a low affinity peptide substrate to a selective and moderately potent inhibitor for these enzymes.

CiteXplore: 15125966

DOI: 10.1016/j.bmcl.2004.03.039