Rapid synthesis of Abelson tyrosine kinase inhibitors using click chemistry

Karunakaran A. Kalesh, Kai Liu, Shao Q. Yao

Research output: Contribution to journalArticlepeer-review


Protein kinases catalyze the phosphorylation of serine, threonine, tyrosine and histidine residues in proteins. Aberrant regulation of kinase activity has been implicated in many diseases including cancer. Thus development of new strategies for kinase inhibitor design remains an active area of research with direct relevance to drug development. Abelson (Abl) tyrosine kinase is one of the Src-family of tyrosine kinases and is directly implicated in Chronic Myelogenous Leukemia (CML). In this article, we have, for the first time, developed an efficient method for the construction of small molecule-based bisubstrate inhibitors of Abl kinase using click chemistry. Subsequent biochemical screenings revealed a set of moderately potent inhibitors, a few of which have comparable potency to Imatinib (an FDA-approved drug for treatment of chronic myeloid leukemia) against Abl.

Original languageEnglish
Pages (from-to)5129-5136
Number of pages8
JournalOrganic & Biomolecular Chemistry
Publication statusPublished - 14 Oct 2009
Externally publishedYes


Dive into the research topics of 'Rapid synthesis of Abelson tyrosine kinase inhibitors using click chemistry'. Together they form a unique fingerprint.

Cite this