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MS31 is a potent, cell permeable, highly affinity, and highly selective fragment-like methyllysine reader protein spindlin 1 (SPIN1) inhibitor, which potently inhibits the interactions between SPIN1 and H3K4me3 (IC50=77 nM, AlphaLISA; 243 nM, FP). It selectively binds Tudor domain II of SPIN1 (Kd=91 nM). MS31 potently inhibits binding of trimethyllysine-containing peptides to SPIN1, and is not toxic to nontumorigenic cells[1]. IC50: 77 nM (SPIN1 by AlphaLISA), 243 nM (SPIN1 by FP)[1]Kd: 91 nM (SPIN1)[1]

MS31 potently inhibits binding of trimethyllysine-containing peptides to SPIN1, displays high binding affinity, is highly selective for SPIN1 over other epigenetic readers and writers, directly engages SPIN1 in cells, and is not toxic to nontumorigenic cells. MS31 selectively binds tudor domain II of SPIN1[1].

[1]. Xiong Y, et al. Discovery of a Potent and Selective Fragment-like Inhibitor of Methyllysine Reader Protein Spindlin 1(SPIN1). J Med Chem. 2019 Jul 24.

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