ChEMBL ligand: CHEMBL483857
MMP2/72 kDa type IV collagenase in Human [ChEMBL: CHEMBL333] [GtoPdb: 1629] [UniProtKB: P08253] There should be some charts here, you may need to enable JavaScript!
ADAM17/Disintegrin and metalloproteinase domain-containing protein 17 in Human [ChEMBL: CHEMBL3706] [GtoPdb: 1662] [UniProtKB: P78536] There should be some charts here, you may need to enable JavaScript!
MMP1/Interstitial collagenase in Human [ChEMBL: CHEMBL332] [GtoPdb: 1628] [UniProtKB: P03956] There should be some charts here, you may need to enable JavaScript!
MMP7/Matrilysin in Human [ChEMBL: CHEMBL4073] [GtoPdb: 1631] [UniProtKB: P09237] There should be some charts here, you may need to enable JavaScript!
MMP14/Matrix metalloproteinase-14 in Human [ChEMBL: CHEMBL3869] [GtoPdb: 1638] [UniProtKB: P50281] There should be some charts here, you may need to enable JavaScript!
MMP9/Matrix metalloproteinase-9 in Human [ChEMBL: CHEMBL321] [GtoPdb: 1633] [UniProtKB: P14780] There should be some charts here, you may need to enable JavaScript!
MMP8/Neutrophil collagenase in Human [ChEMBL: CHEMBL4588] [GtoPdb: 1632] [UniProtKB: P22894] There should be some charts here, you may need to enable JavaScript!
MMP3/Stromelysin-1 in Human [ChEMBL: CHEMBL283] [GtoPdb: 1630] [UniProtKB: P08254] There should be some charts here, you may need to enable JavaScript!

DB	Assay description	Assay Type	Standard value	Standard parameter	Original value	Original units	Original parameter	Reference
MMP2/72 kDa type IV collagenase in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL333] [GtoPdb: 1629] [UniProtKB: P08253]
ChEMBL	Inhibition of recombinant human MMP2	B	7.55	pKi	28	nM	Ki	J Med Chem (2018) 61: 8825-8837 [PMID:30212201]
ChEMBL	Inhibition of MMP-2 (unknown origin)	B	7.55	pKi	28	nM	Ki	J Med Chem (2022) 65: 10709-10754 [PMID:35969157]
ChEMBL	Competitive inhibition of human MMP-2 assessed as inhibition constant	B	7.85	pKi	14	nM	Ki	Eur J Med Chem (2021) 223: 113623-113623 [PMID:34157437]
ChEMBL	Competitive inhibition of human MMP2 using fluorogenic substrate by Dixon plot analysis	B	7.86	pKi	13.9	nM	Ki	ACS Med Chem Lett (2012) 3: 490-495 [PMID:22737278]
ChEMBL	Inhibition of MMP2	B	7.86	pKi	13.9	nM	Ki	Bioorg Med Chem (2008) 16: 8781-8794 [PMID:18790648]
ChEMBL	Inhibition of recombinant human MMP2 expressed in human HeLaS3 cells using MOCAcPLGLA2pr(Dnp)-AR-NH2 as substrate incubated for 15 to 30 mins by fluorescence method	B	7.86	pKi	13.9	nM	Ki	J Med Chem (2020) 63: 10705-10725 [PMID:32459966]
ChEMBL	Inhibition of MMP2 by substrate hydrolysis based fluorescence spectrophotometry	B	7.86	pKi	13.9	nM	Ki	ACS Med Chem Lett (2011) 2: 177-181 [PMID:24900296]
GtoPdb	-	-	7.86	pKi	13.9	nM	Ki	J Am Chem Soc (2000) 122: 6799-6800
ChEMBL	Inhibition of MMP-2 (unknown origin)	B	7.55	pIC50	28	nM	IC50	J Med Chem (2021) 64: 2851-2877 [PMID:33656892]
ADAM17/Disintegrin and metalloproteinase domain-containing protein 17 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3706] [GtoPdb: 1662] [UniProtKB: P78536]
ChEMBL	Inhibition of TACE	B	5.43	pKi	3700	nM	Ki	Bioorg Med Chem (2008) 16: 8781-8794 [PMID:18790648]
MMP1/Interstitial collagenase in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL332] [GtoPdb: 1628] [UniProtKB: P03956]
ChEMBL	Inhibition of MMP-1 (unknown origin)	B	4.14	pKi	73000	nM	Ki	J Med Chem (2022) 65: 10709-10754 [PMID:35969157]
MMP7/Matrilysin in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4073] [GtoPdb: 1631] [UniProtKB: P09237]
ChEMBL	Inhibition of MMP7	B	4.02	pKi	96000	nM	Ki	Bioorg Med Chem (2008) 16: 8781-8794 [PMID:18790648]
ChEMBL	Inhibition of human recombinant MMP7 catalytic domain by substrate hydrolysis based fluorescence spectrophotometry	B	4.02	pKi	96000	nM	Ki	ACS Med Chem Lett (2011) 2: 177-181 [PMID:24900296]
ChEMBL	Competitive inhibition of human MMP7 using fluorogenic substrate by Dixon plot analysis	B	4.02	pKi	96000	nM	Ki	ACS Med Chem Lett (2012) 3: 490-495 [PMID:22737278]
ChEMBL	Inhibition of MMP-7 (unknown origin)	B	4.17	pKi	67000	nM	Ki	J Med Chem (2022) 65: 10709-10754 [PMID:35969157]
MMP14/Matrix metalloproteinase-14 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3869] [GtoPdb: 1638] [UniProtKB: P50281]
ChEMBL	Inhibition of human recombinant MMP14 catalytic domain by substrate hydrolysis based fluorescence spectrophotometry	B	6.96	pKi	110	nM	Ki	ACS Med Chem Lett (2011) 2: 177-181 [PMID:24900296]
ChEMBL	Inhibition of MMP-14 (unknown origin)	B	6.96	pKi	110	nM	Ki	J Med Chem (2022) 65: 10709-10754 [PMID:35969157]
ChEMBL	Competitive inhibition of human MMP14 using fluorogenic substrate by Dixon plot analysis	B	7.43	pKi	37	nM	Ki	ACS Med Chem Lett (2012) 3: 490-495 [PMID:22737278]
MMP9/Matrix metalloproteinase-9 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL321] [GtoPdb: 1633] [UniProtKB: P14780]
ChEMBL	Enzyme Inhibition Assay: Human recombinant active MMP-2 and MMP-7, and the catalytic domains of MMP-3 and MMP-14/MT1-MMP were purchased from EMD Chemicals, Inc. (San Diego, Calif., USA); human recombinant catalytic domains of MMP-1, MMP-8, and MMP-9 were purchased from Enzo Life Sciences, Inc. (Farmingdale, N.Y., USA); human recombinant active ADAM9 and ADAM10 were purchased from R&D Systems (Minneapolis, Minn., USA). Fluorogenic substrates MOCAc-Pro-Leu-Gly-Leu-A2pr(Dnp)-Ala-Arg-NH2 (for MMP-2, MMP-7, MMP-9 and MMP-14) and MOCAc-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 (for MMP-3) were purchased from Peptides International (Louisville, Ky., USA); Mca-KPLGL-Dpa-AR-NH2 (for MMP-1, MMP-8 and ADAM10) and Mca-PLAQAV-Dpa-RSSSR-NH2 (for ADAM9) were purchased from R&D Systems (Minneapolis, Minn., USA). The Km values for MMP-2, MMP-9 and MMP-14 were the same as previously reported by Gooyit et al. ((2013) J. Med. Chem. 56(20):8139-8150). Inhibitor stock solutions (10 mM) were prepared freshly in DMSO before enzyme inhibition assays. We followed the same methodology for enzyme inhibition studies as reported before by Page-McCaw et al. ((2007) Nat Rev Mol Cell Biol 8(3):221-233). Enzyme inhibition studies were carried out using a Cary Eclipse fluorescence spectrophotometer (Varian, Walnut Creek, Calif., USA). Compound 1 was stable in the buffers used in the kinetic assays.	B	5.68	pKi	2100	nM	Ki	US-10357546-B2. Acceleration of diabetic wound healing (2019)
GtoPdb	-	-	6.22	pKi	600	nM	Ki	J Am Chem Soc (2000) 122: 6799-6800
ChEMBL	Inhibition of human recombinant MMP9 catalytic domain by substrate hydrolysis based fluorescence spectrophotometry	B	6.22	pKi	600	nM	Ki	ACS Med Chem Lett (2011) 2: 177-181 [PMID:24900296]
ChEMBL	Competitive inhibition of human MMP9 using fluorogenic substrate by Dixon plot analysis	B	6.22	pKi	600	nM	Ki	ACS Med Chem Lett (2012) 3: 490-495 [PMID:22737278]
ChEMBL	Inhibition of MMP9	B	6.22	pKi	600	nM	Ki	Bioorg Med Chem (2008) 16: 8781-8794 [PMID:18790648]
ChEMBL	Inhibition of recombinant human MMP9 expressed in human HeLaS3 cells using MOCAcPLGLA2pr(Dnp)-AR-NH2 as substrate incubated for 15 to 30 mins by fluorescence method	B	6.22	pKi	600	nM	Ki	J Med Chem (2020) 63: 10705-10725 [PMID:32459966]
ChEMBL	Competitive inhibition of human MMP-9 assessed as inhibition constant	B	6.22	pKi	600	nM	Ki	Eur J Med Chem (2021) 223: 113623-113623 [PMID:34157437]
ChEMBL	Inhibition of recombinant human MMP9	B	6.4	pKi	400	nM	Ki	J Med Chem (2018) 61: 8825-8837 [PMID:30212201]
ChEMBL	Inhibition of MMP-9 (unknown origin)	B	6.4	pKi	400	nM	Ki	J Med Chem (2022) 65: 10709-10754 [PMID:35969157]
ChEMBL	Inhibition of MMP-9 (unknown origin)	B	6.4	pIC50	400	nM	IC50	J Med Chem (2021) 64: 2851-2877 [PMID:33656892]
MMP8/Neutrophil collagenase in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4588] [GtoPdb: 1632] [UniProtKB: P22894]
ChEMBL	Non-competitive inhibition of MMP8 (unknown origin)	B	5.68	pKi	2100	nM	Ki	J Med Chem (2018) 61: 8825-8837 [PMID:30212201]
ChEMBL	Enzyme Inhibition Assay: Human recombinant active MMP-2 and MMP-7, and the catalytic domains of MMP-3 and MMP-14/MT1-MMP were purchased from EMD Chemicals, Inc. (San Diego, Calif., USA); human recombinant catalytic domains of MMP-1, MMP-8, and MMP-9 were purchased from Enzo Life Sciences, Inc. (Farmingdale, N.Y., USA); human recombinant active ADAM9 and ADAM10 were purchased from R&D Systems (Minneapolis, Minn., USA). Fluorogenic substrates MOCAc-Pro-Leu-Gly-Leu-A2pr(Dnp)-Ala-Arg-NH2 (for MMP-2, MMP-7, MMP-9 and MMP-14) and MOCAc-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 (for MMP-3) were purchased from Peptides International (Louisville, Ky., USA); Mca-KPLGL-Dpa-AR-NH2 (for MMP-1, MMP-8 and ADAM10) and Mca-PLAQAV-Dpa-RSSSR-NH2 (for ADAM9) were purchased from R&D Systems (Minneapolis, Minn., USA). The Km values for MMP-2, MMP-9 and MMP-14 were the same as previously reported by Gooyit et al. ((2013) J. Med. Chem. 56(20):8139-8150). Inhibitor stock solutions (10 mM) were prepared freshly in DMSO before enzyme inhibition assays. We followed the same methodology for enzyme inhibition studies as reported before by Page-McCaw et al. ((2007) Nat Rev Mol Cell Biol 8(3):221-233). Enzyme inhibition studies were carried out using a Cary Eclipse fluorescence spectrophotometer (Varian, Walnut Creek, Calif., USA). Compound 1 was stable in the buffers used in the kinetic assays.	B	6.4	pKi	400	nM	Ki	US-10357546-B2. Acceleration of diabetic wound healing (2019)
MMP3/Stromelysin-1 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL283] [GtoPdb: 1630] [UniProtKB: P08254]
ChEMBL	Inhibition of MMP3	B	4.82	pKi	15000	nM	Ki	Bioorg Med Chem (2008) 16: 8781-8794 [PMID:18790648]
ChEMBL	Inhibition of human recombinant MMP3 catalytic domain by substrate hydrolysis based fluorescence spectrophotometry	B	4.82	pKi	15000	nM	Ki	ACS Med Chem Lett (2011) 2: 177-181 [PMID:24900296]
ChEMBL	Competitive inhibition of human MMP3 using fluorogenic substrate by Dixon plot analysis	B	4.82	pKi	15000	nM	Ki	ACS Med Chem Lett (2012) 3: 490-495 [PMID:22737278]
ChEMBL	Inhibition of MMP-3 (unknown origin)	B	5.4	pKi	4000	nM	Ki	J Med Chem (2022) 65: 10709-10754 [PMID:35969157]

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]