Shilin Xu, Angelo Aguilar, Liyue Huang, Tianfeng Xu, Ke Zheng, Donna McEachern, Sally Przybranowski, Caroline Foster, Kaitlin Zawacki, Zhaomin Liu, Krishnapriya Chinnaswamy, Jeanne Stuckey, and Shaomeng Wang
Journal of Medicinal Chemistry, 2020
DOI: 10.1021/acs.jmedchem.0c00547
Targeting the menin–MLL protein–protein interaction is a new therapeutic strategy for the treatment of acute leukemia carrying MLL fusion (MLL leukemia). We describe herein the structure-based optimization of a class of covalent menin inhibitors, which led to the discovery of M-808 (16) as a highly potent and efficacious covalent menin inhibitor. M-808 effectively inhibits leukemia cell growth at low nanomolar concentrations and is capable of achieving partial tumor regression in an MV4;11 xenograft tumor model in mice at a well-tolerated dose schedule. Determination of the co-crystal structure of M-808 in complex with menin provides a structural basis for their high-affinity, covalent interactions. M-808 represents a promising, covalent menin inhibitor for further optimization and evaluation toward developing a new therapy for the treatment of MLL leukemia.
A blog highlighting recent publications in the area of covalent modification of proteins, particularly relating to covalent-modifier drugs. @CovalentMod on Twitter, @covalentmod@mstdn.science on Mastodon, and @covalentmod.bsky.social on BlueSky
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