TNP-GTP (sodium salt)

TNP-GTP is a fluorescent derivative of the energy substrate for protein synthesis and gluconeogenesis, guanosine 5'-triphosphate (GTP; Item No. 16060).¹ It displays an emission maximum of 552 nm upon excitation at 410 nm in water, with fluorescence increasing in intensity and shifting to 544 and 532 nm in 40 and 80% N,N-dimethylformamide, respectively, which is less polar than water.¹ TNP-GTP is an inhibitor of glutamate dehydrogenase (K_i = 2.7 μM). When bound to glutamate dehydrogenase, the fluorescence intensity of TNP-GTP is increased and the emission shifts from 552 to 545 nm, an effect that can be blocked by addition of GTP. TNP-GTP is an antagonist of the purinergic P2X₂ and P2X_2/3 receptors (IC₅₀s = 0.4 and 1.2 nM, respectively).² It also selectively inhibits rat soluble guanylyl cyclase (sGC; K_i = 11 nM) over bovine liver glutamate dehydrogenase (GDH; K_i = 2.7 µM) and the calmodulin-dependent B. pertussis adenylyl cyclase (AC) toxin (K_is = 20 and 320 µM in the presence of manganese or magnesium, respectively).^3,1,4

WARNING This product is not for human or veterinary use.

1. Hiratsuka, T. A chromophoric and fluorescent analog of GTP, 2',3'-O-(2,4,6-trinitrocyclohexadienylidene)-GTP, as a spectroscopic probe for the GTP inhibitory site of liver glutamate dehydrogenase. The Journal of Biological Chemisty 260(8), 4784-4790 (1985).

2. Virginio, C., Robertson, G., Surprenant, A., et al. Trinitrophenyl-substituted nucleotides are potent antagonists selective for P2X1, P2X3, and heteromeric P2X2/3 receptors. Mol. Pharmacol. 53(6), 969-973 (1998).

3. Dove, S., Danker, K.Y., Stasch, J.-P., et al. Structure/activity relationships of (M)ANT- and TNP-nucleotides for inhibition of rat soluble guanylyl cyclase α1β1. Mol. Pharmacol. 85(4), 598-607 (2014).

4. Göttle, M., Dove, S., Steindel, P., et al. Molecular analysis of the interaction of Bordetella pertussis adenylyl cyclase with fluorescent nucleotides. Mol. Pharmacol. 72(3), 526-535 (2007).