IGGi-11

IGGi-11 binds to the GIV interacting region of wild-type Gαi3 with low micromolar affinity, confirming the specific binding site is localized to the groove between the α3 helix and Switch II region of the protein^[1].
IGGi-11 inhibits the GIV-Gαi interaction across all three members of the Gαi protein family in vitro with low micromolar potency^[1].
IGGi-11 blocks GIV-mediated enhancement of Gαi3 nucleotide exchange and subsequent GTP hydrolysis in a cell-free system^[1].
IGGi-11 (500 μM) binds to truncated human sGαi3 at 298 K with a K_d of 5.3 μM, confirming that removal of the flexible terminal residues of Gαi3 does not alter the binding affinity for IGGi-11^[2].
IGGi-11 induces an identical pattern of NMR signal perturbations in sGαi3 as in full-length Gαi3, demonstrating that the binding interface for IGGi-11 is fully preserved in the truncated protein construct^[2].
IGGi-11 results in two distinct, stable, non-exclusive binding modes for IGGi-11 due to the symmetric chemical structure of IGGi-11 and the elongated, flexible shape of the binding cleft on sGαi3, which explains the observed heterogeneity of molecular recognition^[2].
IGGi-11 selectively disrupts the GIV-Gαi protein-protein interaction at micromolar affinity without altering any canonical Gαi-mediated GPCR signaling pathways in a cell-free biochemical system^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.