Methyl (S)-2-(4-(4'-((4-(N-(3-cyano-4-methyl-1H-indol-7-yl)sulfamoyl)benzyl)carbamoyl)-[1,1'-biphenyl]-4-yl)-2,3,9-trimethyl-6H-thieno[3,2-f][1,2,4]triazolo[4,3-a][1,4]diazepin-6-yl)acetate

IBG1 (0.01-1 μM; 22 h) potently degrades BRD4 in both PSMA-negative PC3 and PSMA-positive PC3-PIP human prostate adenocarcinoma cells with a sub-nanomolar DC₅₀^[2].
IBG1 selectively stabilizes the BRD4-DCAF16 ternary complex over BRD3-DCAF16 via BRD4 residue G386, with binding free energy changes from mutations matching experimentally observed degradation selectivity^[3].
IBG1 acts as an intramolecular bivalent glue to bridge BRD4's BD1 and BD2 bromodomains, stabilizing a BRD4:DCAF16 interaction (K_d = 1.5 μM) with high cooperativity to drive selective degradation of BRD4 and BRD2^[4].
IBG1 (0.01-1 μM; 22 h) potently degrades BRD4 with sub-nanomolar potency in PC3 and PC3-PIP prostate cancer cells^[5].
IBG1 (16 h) does not covalently modify DCAF16 in the presence or absence of recombinant BRD4_tandem^[6].
IBG1 (1 μM; 16 h) induces BRD4 degradation in DCAF16-knockout K562 cells expressing wild-type DCAF16, DCAF16^(C58S), or DCAF16^(A53R), but not in cells expressing DCAF16^(C177S) or DCAF16^(C179S)[6].
IBG1 (0.001-10 μM; 16 h) induces dose-dependent degradation of BRD4_tandem-eGFP in DCAF16-knockout K562 cells expressing wild-type DCAF16 or DCAF16^C58S, but not in cells expressing DCAF16^C177S or DCAF16^C179S[6].
IBG1 enhances the intrinsic affinity between BRD4 and DCAF16, binds at the DCAF16/BRD4 BD1/BD2 interface to form a stable ternary complex with DDB1, and acts as an intramolecular bivalent glue to degrade BRD4 via DCAF16-mediated recruitment to the E3 ligase complex^[7].
IBG1 (0.1-1000 nM; 6 h) potently degrades BRD2 and BRD4, but not BRD3, in HEK293 cells^[8].
IBG1 (1 nM; 6 h) selectively downregulates BRD4 and BRD2 in KBM7 cells^[8].
IBG1 (0.01-1 μM; 25 h) induces rapid, concentration-dependent degradation of BRD4 in BromoTag-HiBiT-BRD4 knock-in HEK293 cells, an effect abrogated by MLN4924 pre-treatment^[8].
IBG1 (0.01-1 μM; 6 h) induces concentration-dependent ubiquitination of BRD4 in LgBiT-transfected HiBiT-BromoTag-BRD4 knock-in HEK293 cells, an effect blocked by NEDD8-activating enzyme inhibitor but not by bromodomain and extra-terminal motif inhibitor or vascular endothelial growth factor receptor inhibitor pre-treatment^[8].
IBG1 (0.1-1000 nM; 6 h) degrades BRD2 and BRD4 in both wild-type and DCAF15-knockout HCT-116 cells, demonstrating DCAF15-independent activity^[8].
IBG1 (1 nM; 6 h)-mediated BRD4 degradation in KBM7 iCas9 BRD4-BFP reporter cells requires the CRL4-DCAF16 complex, but not DCAF15^[8].
Resistance to IBG1 (58 nM; 6 days)-induced cell death in HCT-116 cells is mediated by the CRL4-DCAF16 complex component DCAF16 and the ubiquitin-conjugating enzyme UBE2G1^[8].
IBG1 promotes formation of a stable ternary complex between BRD4Tandem and DCAF16-DDB1(ΔBPB)-DDA1 with a K_d of 567 nM, as measured by ITC^[8].
IBG1 (increasing concentrations; 30 min) promotes dose-dependent formation of the BRD4_Tandem-DCAF16 ternary complex with an EC₅₀ of 44 nM, as measured by TR-FRET^[8].
IBG1 (1 μM; 30 min) enhances the intrinsic interaction between BRD4_Tandem and DCAF16 (K_d = 712 nM in presence of IBG1 vs. 1 μM in absence), while no interaction occurs between DCAF16 and isolated BRD4 bromodomains^[8].
IBG1 (ex vivo; 50 min) stabilizes the formation of a ternary complex between BRD4Tandem and DCAF16-DDB1(ΔBPB)-DDA1, as shown by SEC co-elution, while isolated BRD4 bromodomains do not form a stable complex with DCAF16 in the presence of IBG1^[8].
IBG1 (increasing concentrations) exhibits significantly higher binding affinity to BRD4_Tandem in the presence of DCAF16 (IC₅₀ = 12.8 nM vs. 462 nM alone), while no such enhancement occurs with isolated BRD4_BD1^[8].
IBG1 (1 nM; 6 h) selectively degrades BRD2Tandem and BRD4Tandem, but not BRD3Tandem or isolated BRD4 bromodomains, in KBM7 reporter cells, with BRD4BD2 being the key determinant of selectivity over BRD3^[8].

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