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Comparative Analysis of Two NNMT Bisubstrate Inhibitors through Chemoproteomic Studies: Uncovering the Role of Unconventional SAM Analogue Moiety for Improved Selectivity

ACS Chem Biol. 2024-01; 
Ying Meng, Iredia D Iyamu, Noha A M Ahmed, Rong Huang
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Proteins, Expression, Isolation and Analysis … state of proteins and maximize solubilization of cellular proteins. … No protein band was detected in the final wash using 150 … N-terminal TEV cleavage site was synthesized by Genscript. … Get A Quote

摘要

Unconventional -adenosyl--methionine (SAM) mimics with enhanced hydrophobicity are an adaptable building block to develop cell-potent inhibitors for SAM-dependent methyltransferases as targeted therapeutics. We recently discovered cell-potent bisubstrate inhibitors for nicotinamide -methyltransferase (NNMT) by using an unconventional SAM mimic. To delve into the selectivity implications of the unconventional SAM mimic, we employed a chemoproteomic approach to assess two potent NNMT inhibitors LL320 ( = 6.8 nM) and II399 (containing an unconventional SAM mimic, = 5.9 nM) within endogenous proteomes. Our work began with the rational design and synthesis of immobilized probes and , utilizing LL320 and II399 as p... More

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