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MIF inhibitors target macrophage migration inhibitory factor, a cytokine with an enzymatic pocket. Macrophage migration inhibitory factor (MIF) was described in 1966 as a lymphocyte product that inhibits macrophage migration in delayed-type hypersensitivity. In 1996, the trimeric protein was found to catalyze a tautomerization reaction. A 2003 study showed that MIF signals by binding to the cell surface protein cluster of differentiation 74 (CD74). 4-IPP and ISO-92 are listed as MIF inhibitors, and MIF098 and (±)-CPSI-1306 as MIF antagonists. MD13 is a proteolysis-targeting chimera (PROTAC) that induces degradation of MIF in cells. 4-CPPC acts on the homolog MIF-2, also called D-dopachrome tautomerase. The set also contains (E/Z)-BCI, a dual-specificity phosphatase 6 (DUSP6) inhibitor.
MD13 is a macrophage migration inhibitory factor (MIF)-directed PROTAC with a Ki of 71 nM. This compound facilitates the targeted degradation of MIF, offering potential utility in cancer research by modulating inflammatory responses associated with tumor progression. Its application may provide insights into therapeutic strategies for malignancies influenced by MIF signaling pathways.
