omarigliptin [Ligand Id: 8402] activity data from GtoPdb and ChEMBL
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| ChEMBL ligand: CHEMBL2105762 (MK-3102, Omarigliptin, Omarigliptina, Omarigliptine) |
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| DB | Assay description | Assay Type | Standard value | Standard parameter | Original value | Original units | Original parameter | Reference |
|---|---|---|---|---|---|---|---|---|
| Dipeptidyl-peptidase 7/Dipeptidyl peptidase 2 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3976] [GtoPdb: 1605] [UniProtKB: Q9UHL4] | ||||||||
| ChEMBL | Inhibition of N-terminal FLAG tagged human QPP expressed in Sf9 cells using Nle-Pro-AMC substrate after 30 mins by plate reader analysis | B | 4 | pIC50 | >100000 | nM | IC50 | Bioorg Med Chem Lett (2015) 25: 5767-5771 [PMID:26546218] |
| ChEMBL | Inhibition of QPP (unknown origin) | B | 4.17 | pIC50 | >67000 | nM | IC50 | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
| dipeptidyl peptidase 4/Dipeptidyl peptidase 4 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL284] [GtoPdb: 1612] [UniProtKB: P27487] | ||||||||
| ChEMBL | Binding affinity to DPP4 (unknown origin) assessed as dissociation constant by SPR assay | B | 8.56 | pKd | 2.75 | nM | Kd | J Med Chem (2016) 59: 6772-6790 [PMID:27396490] |
| ChEMBL | Binding affinity to DPP4 (unknown origin) expressed in baculovirus expressing system | B | 8.56 | pKd | 2.75 | nM | Kd | J Med Chem (2019) 62: 2348-2361 [PMID:30694668] |
| ChEMBL | Competitive reversible inhibition of DPP4 (unknown origin) | B | 9.1 | pKi | 0.8 | nM | Ki | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
| GtoPdb | - | - | 9.1 | pKi | 0.8 | nM | Ki | J Med Chem (2014) 57: 3205-12 [PMID:24660890] |
| ChEMBL | DPP-IV Inhibitory Activity: 1. DPP-IV enzyme reaction buffer was prepared (50 mM HEPES (pH=7.8), 80 mM MgCl2, 150 mM NaCl, 1% BSA), and stored on ice for use; 2. The test compounds were diluted with DMSO from 10 mM to 1 mM (100-fold final concentration), and then diluted gradiently 3 folds in a 96-well plate to obtain 11 concentrations; DMSO was added to the twelfth well as a blank control, and then diluted 25 folds with the enzyme reaction buffer to 4-fold final concentration for use; 3. The DPP-IV enzyme reaction substrate H-Gly-Pro-AMC was thawed and diluted to 160 uM (4-fold final concentration) with the enzyme reaction buffer, and then stored on ice for use; 4. The rat plasma was thawed and diluted 100 folds (2-fold final concentration) with the enzyme reaction buffer, and then stored on ice for use; 5. 5 uL of the test compounds (4-fold final concentration) were added to a 384-well plate, and then L of the rat plasma (2-fold final concentration) was added, centrifuged and mixed well; 6. 5 uL of the enzyme reaction substrate H-Gly-Pro-AMC (4-fold final concentration) was added, centrifuged and mixed well, and then the 384-well plate was sealed with a film; 7. The resulting mixture was incubated in an incubator (22-23 C.) for 1 hour; 8. The fluorescence signal was determined using FlexStationI3 (Molecular devices) microplate reader (excited at 380 nm, and the emission spectrum was determined at 460 nm wavelength); 9. IC50 values of the test compounds in inhibiting DPP-IV activity were determined, i.e., calculating the IC50 values of the compounds using GraFit6 software. | B | 8.38 | pIC50 | 4.2 | nM | IC50 | US-10155775-B2. Substituted amino six-membered saturated heteroalicycles as long-acting DPP-IV inhibitors (2018) |
| ChEMBL | Inhibition of human recombinant DPP4 incubated for 15 mins using Gly-Pro-7-AMC substrate | B | 8.51 | pIC50 | 3.1 | nM | IC50 | J Med Chem (2020) 63: 7108-7126 [PMID:32452679] |
| ChEMBL | Inhibition of recombinant human DPP4 expressed in Sf9 cells using Gly-Pro-AMC substrate after 30 mins by plate reader analysis | B | 8.59 | pIC50 | 2.6 | nM | IC50 | Bioorg Med Chem Lett (2015) 25: 5767-5771 [PMID:26546218] |
| ChEMBL | Inhibition of DPP4 (unknown origin) expressed in Sf9 cells using Gly-Pro-AMC substrate | B | 8.65 | pIC50 | 2.22 | nM | IC50 | J Med Chem (2016) 59: 6772-6790 [PMID:27396490] |
| ChEMBL | Inhibition Activity Assay: Screening Method:Name of method: Activity Evaluation of DPP4, Fluorescence.Instrument: Microplate reader, Envision (PerkinElmer, USA).Material: human DPP4, which was, in this experiment, obtained by using baculovirus expression system in insect cells. Substrate was Gly-Pro-AMC.Process:DPP4 can specifically hydrolyze the substrate, Gly-Pro-AMC to produce a product, AMC, which, excited by UV light at 355 nm, can produce emission light at 460 nm. Linear change of fluorescence values were dynamically measured at 460 nm wavelengths per unit time, thereby calculating DPP4 activity. MERK-0431 was used as a control compound in the experiment. | B | 8.7 | pIC50 | 2 | nM | IC50 | US-10479798-B2. Six-membered ring benzo derivatives as DPP-4 inhibitor and use thereof (2019) |
| ChEMBL | Inhibition of DPP-4 (unknown origin) | B | 8.8 | pIC50 | 1.6 | nM | IC50 | J Med Chem (2023) 66: 11593-11631 [PMID:37647598] |
| ChEMBL | Competitive reversible inhibition of DPP4 (unknown origin) | B | 8.8 | pIC50 | 1.6 | nM | IC50 | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
| ChEMBL | Inhibition of human recombinant DPP-4 (1 to 530 residues) using Gly-Pro-AMC as substrate preincubated for 30 mins followed by substrate addition measured after 5 mins by CF assay | B | 8.8 | pIC50 | 1.6 | nM | IC50 | J Med Chem (2023) 66: 11593-11631 [PMID:37647598] |
| ChEMBL | Inhibition of DPP-4 (unknown origin) | B | 8.6 | pEC50 | 2.5 | nM | EC50 | J Med Chem (2023) 66: 11593-11631 [PMID:37647598] |
| dipeptidyl peptidase 4/Dipeptidyl peptidase 4 in Mouse (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3883] [GtoPdb: 1612] [UniProtKB: P28843] | ||||||||
| ChEMBL | Inhibition of DPP4 in mouse plasma | B | 7.36 | pIC50 | 43.9 | nM | IC50 | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
| dipeptidyl peptidase 4/Dipeptidyl peptidase 4 in Rat (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4653] [GtoPdb: 1612] [UniProtKB: P14740] | ||||||||
| ChEMBL | Inhibition Enzyme Activity Assay: a. White 384-well plate (Perkin Elmer, Catalog No. 607290/99)b. HEPES buffer: using 1M HEPES buffer (Invitrogen, Catalog No. 15630-080) to prepare 50 ml of 0.5M HEPES buffer by following the steps of taking 25 mL of 1 M HEPES buffer, adding an appropriate amount of ddH2O (re-distilled water), adjusting the pH to 7.8 with NaOH, and finally adding ddH2O to 50 mL.c. Rat plasma: taking blood samples from rat orbit, adding heparin for anticoagulation, centrifuging for 10 minutes at 4000 rpm, taking supernatant plasma as an enzyme source of DPP-IV.d. H-Gly-Pro-AMC (glycine-proline-7-amino-4-methylcoumarin) as the enzyme reaction substrate of DPP-IV, which was synthesized by one of the applicants, was dissolved in DMSO to form 100 mM mother solution.e. 1M MgCl2f. 1.5M NaClg. 10% BASh. DMSO (dimethylsulphoxide)i. ddH2Oj. Test compounds: Omarigliptin as a positive control compound and the compound represented by Formula I of the present application.Following the Sequence Below:1. DPP-IV enzyme reaction buffer was prepared (50 mM HEPES (pH=7.8), 80 mM MgCl2, 150 mM NaCl, 1% BSA), and stored on ice for use:2. The test compounds were diluted with DMSO from 10 mM to 1 mM (100-fold final working concentration), and then diluted gradiently 3 folds in a 96-well plate to obtain 11 concentrations; DMSO was added to the twelfth well as a blank control, and then diluted 25 folds with the enzyme reaction buffer to 4-fold final working concentration for use;3. The DPP-IV enzyme reaction substrate H-Gly-Pro-AMC was thawed and diluted to 160 μM (4-fold working concentration) with the enzyme reaction buffer, and then stored on ice for use:4. The rat plasma was thawed and diluted 100 folds (2-fold working concentration) with the enzyme reaction buffer, and then stored on ice for use;5. 5 μL of the test compounds (4-fold concentration) were added to a 384-well plate, and then 10 μL of the rat plasma (2-fold working concentration) was added, centrifuged and mixed well:6. 5 μL of the enzyme reaction substrate H-Gly-Pro-AMC (4-fold working concentration) was added, centrifuged and mixed well, and then the 384-well plate was sealed with a film:7. The resulting mixture was incubated in an incubator (22-23° C.) for 1 hour:8. The fluorescence signal was determined using FlexStation13 (Molecular devices) microplate reader (excited at 380 nm, and the emission spectrum was determined at 460 nm wavelength);9. IC50 values of the test compounds in inhibiting DPP-IV enzyme activity were determined, i.e., calculating the IC50 values of the compounds using GraFit6 software. | B | 8.38 | pIC50 | 4.2 | nM | IC50 | US-10822319-B2. Crystal of DPP-IV long-acting inhibitor and salt (2020) |
| dipeptidyl peptidase 8/Dipeptidyl peptidase 8 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4657] [GtoPdb: 2356] [UniProtKB: Q6V1X1] | ||||||||
| ChEMBL | Inhibition of C-terminal His-tagged DPP8 (unknown origin) expressed in COS7 cells using H-Ala-Pro-pNA substrate preincubated for 15 mins | B | 4 | pIC50 | >100000 | nM | IC50 | Bioorg Med Chem Lett (2015) 25: 5767-5771 [PMID:26546218] |
| ChEMBL | Inhibition of DPP8 (unknown origin) | B | 4.17 | pIC50 | >67000 | nM | IC50 | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
| dipeptidyl peptidase 9/Dipeptidyl peptidase 9 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4793] [GtoPdb: 2357] [UniProtKB: Q86TI2] | ||||||||
| ChEMBL | Inhibition of DPP9 (unknown origin) | B | 4.17 | pIC50 | >67000 | nM | IC50 | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
| prolyl endopeptidase/Prolyl endopeptidase in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3202] [GtoPdb: 2395] [UniProtKB: P48147] | ||||||||
| ChEMBL | Inhibition of PEP (unknown origin) | B | 4.17 | pIC50 | >67000 | nM | IC50 | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
| fibroblast activation protein alpha/Prolyl endopeptidase FAP in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4683] [GtoPdb: 2365] [UniProtKB: Q12884] | ||||||||
| ChEMBL | Inhibition of FAP (unknown origin) | B | 4.17 | pIC50 | >67000 | nM | IC50 | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
| Prolyl endopeptidase FAP in Bovine (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3734641] [UniProtKB: A5D7B7] | ||||||||
| ChEMBL | Inhibition of bovine serum FAP | B | 4 | pIC50 | >100000 | nM | IC50 | Bioorg Med Chem Lett (2015) 25: 5767-5771 [PMID:26546218] |
| Nav1.5/Sodium channel protein type 5 subunit alpha in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1980] [GtoPdb: 582] [UniProtKB: Q14524] | ||||||||
| ChEMBL | Inhibition of Nav1.5 (unknown origin) | B | 4.52 | pIC50 | >30000 | nM | IC50 | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
| Cav1.2/Voltage-dependent L-type calcium channel subunit alpha-1C in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1940] [GtoPdb: 529] [UniProtKB: Q13936] | ||||||||
| ChEMBL | Inhibition of Cav1.2 (unknown origin) | B | 4.52 | pIC50 | >30000 | nM | IC50 | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
| ChEMBL | Inhibition of potassium channel Cav1.2 (unknown origin) | B | 4.52 | pIC50 | >30000 | nM | IC50 | Bioorg Med Chem Lett (2015) 25: 5767-5771 [PMID:26546218] |
| Kv11.1/Voltage-gated inwardly rectifying potassium channel KCNH2 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL240] [GtoPdb: 572] [UniProtKB: Q12809] | ||||||||
| ChEMBL | Inhibition of human ERG assessed as reduction in IKr current | B | 4.41 | pIC50 | 39000 | nM | IC50 | Bioorg Med Chem Lett (2015) 25: 5767-5771 [PMID:26546218] |
| ChEMBL | Inhibition of human ERG by MK-499 displacement binding analysis | B | 4.52 | pIC50 | >30000 | nM | IC50 | J Med Chem (2014) 57: 3205-3212 [PMID:24660890] |
ChEMBL data shown on this page come from version 36:
Zdrazil B, Felix E, Hunter F, Manners EJ, Blackshaw J, Corbett S, de Veij M, Ioannidis H, Lopez DM, Mosquera JF, Magarinos MP, Bosc N, Arcila R, Kizilören T, Gaulton A, Bento AP, Adasme MF, Monecke P, Landrum GA, Leach AR. (2024). The ChEMBL Database in 2023: a drug discovery platform spanning multiple bioactivity data types and time periods. Nucleic Acids Res., 52(D1). DOI: 10.1093/nar/gkad1004. [EPMCID:10767899] [PMID:37933841]
Davies M, Nowotka M, Papadatos G, Dedman N, Gaulton A, Atkinson F, Bellis L, Overington JP. (2015) 'ChEMBL web services: streamlining access to drug discovery data and utilities.' Nucleic Acids Res., 43(W1). DOI: 10.1093/nar/gkv352. [EPMCID:25883136]
