N-methylmesoporphyrin

N-methylmesoporphyrin (NMM) is a synthetic porphyrin derivative and a member of the porphyrins class. It is primarily used as an experimental tool in research settings. Mechanistically it acts as a potent inhibitor of ferrochelatase—the enzyme responsible for catalyzing the insertion of iron into protoporphyrin IX during heme biosynthesis[1][4]. Additionally, NMM exhibits high selectivity for binding to G-quadruplex DNA structures over duplex or triplex DNA. Upon binding to G-quadruplexes (notably in telomeric and oncogene promoter regions), it stabilizes these structures and becomes highly fluorescent—making it valuable as a fluorescent probe for studying nucleic acid conformations and interactions[5][8]. Its applications include cancer research (due to its effects on gene expression via GQ stabilization), diagnostics (as a light-up probe), and studies on heme metabolism inhibition[5][9]. It is not approved for clinical use in humans.

Other names

8,13-diethyl-3,7,12,17,23-pentamethyl-21H,23H-porphine-2,18-dipropanoic acid3-[18-(2-carboxyethyl)-7,12-diethyl-3,8,13,17,22-pentamethyl-23H-porphyrin-2-yl]propanoic acidSCHEMBL13325428SCHEMBL-13325428SCHEMBL 13325428SCHEMBL18428599SCHEMBL-18428599SCHEMBL 18428599DTXSID70349630DTXSID-70349630DTXSID 70349630