Language

English

Publication Date

5-11-2023

Journal

ACS Medicinal Chemistry Letters

DOI

10.1021/acsmedchemlett.3c00029

PMID

37197477

PMCID

PMC10184151

PubMedCentral® Posted Date

4-17-2023

PubMedCentral® Full Text Version

Post-print

Abstract

The mitogen-activated protein kinase signaling cascade is conserved across eukaryotes, where it plays a critical role in the regulation of activities including proliferation, differentiation, and stress responses. This pathway propagates external stimuli through a series of phosphorylation events, which allows external signals to influence metabolic and transcriptional activities. Within the cascade, MEK, or MAP2K, enzymes occupy a molecular crossroads immediately upstream to significant signal divergence and cross-talk. One such kinase, MAP2K7, also known as MEK7 and MKK7, is a protein of great interest in the molecular pathophysiology underlying pediatric T cell acute lymphoblastic leukemia (T-ALL). Herein, we describe the rational design, synthesis, evaluation, and optimization of a novel class of irreversible MAP2K7 inhibitors. With a streamlined one-pot synthesis, favorable in vitro potency and selectivity, and promising cellular activity, this novel class of compounds wields promise as a powerful tool in the study of pediatric T-ALL.

Keywords

mitogen-activated protein kinases, drug discovery, small molecule inhibitors, lead optimization, covalent inhibitors, irreversible inhibitors, T cell acute lymphoblastic leukemia, MAP2K7, MEK7, MKK7

Published Open-Access

yes

ml3c00029_0011.jpg (99 kB)
Graphical Abstract

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