1,10-Phenanthroline [Ligand Id: 12425] activity data from GtoPdb and ChEMBL
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| ChEMBL ligand: CHEMBL415879 |
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| 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 | In vitro MMP-8 Assay: The synthetic octapeptide substrate, containing the collagenase-susceptible glycine-isoleucine peptide bond, was incubated (37° C.) with commercially-available chromatrographically-purified human neutrophil collagenase (MMP-8) in the presence of 1 mM Ca++ and the tripeptide degradation fragment and undegraded substrate were separated and measured by HPLC (Waters Alliance 2695 System with a reverse phase C-18 column). | B | 4.15 | pIC50 | 70000 | nM | IC50 | US-9187406-B2. Curcumin analogues as zinc chelators and their uses (2015) |
| ChEMBL | Inhibition of MMPs: It has been observed that 50 and 100 μM concentrations of curcumin decreased TNFα production by endotoxin-stimulated human monocytes (HMs) in culture by 80-90% (lower concentrations of curcumin, 10 and 20 μM, had no effect). However, this inhibitory effect was associated with some precipitation of the curcumin in cell culture and with significant cytotoxicity. It was hypothesized that increasing the solubility of curcumin will: (i) enhance its efficacy as an inhibitor of cytokine expression, (ii) reduce its cytotoxicity, and (iii) preserve (perhaps even enhance; see below) its potency, as an MMP inhibitor (MMPI) compound, which was found to be similar to that of the Zn++ chelating compound, 1,10-O-phenanthroline (FIG. 1). However, it should be noted that excessive inhibition of MMP activity may not be desirable therapeutically because a minimal, or basal, level of MMPs may be necessary for optimal defense of the host. | B | 4.15 | pIC50 | 70000 | nM | IC50 | US-10669227-B2. Curcumin analogues as zinc chelators and their uses (2020) |
| ChEMBL | Inhibition Assay: Table 10: The efficacy of MMP-2 inhibition was as follows: compound 6>compound 7>compound 8. Although compound 6 showed similar efficacy as curcumin when comparing MMP-2 inhibitory potency, the amide-containing compounds are much more soluble than the famously insoluble curcumin. The amide-containing curcumin derivatives are much more potent inhibitors of MMP-13 (Collagenase-3) than curcumin and even more potent than compound 1 (Table 9 and 10).: | B | 4.15 | pIC50 | 70000 | nM | IC50 | US-11608309-B2. Curcumin analogues as zinc chelators and their uses (2023) |
| Beta-lactamase VIM-1 in Pseudomonas aeruginosa (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1287601] [UniProtKB: Q9XAY4] | ||||||||
| ChEMBL | Inhibition of Pseudomonas aeruginosa VIM-1 beta-lactamase after 10 mins | B | 4.14 | pIC50 | 73000 | nM | IC50 | Antimicrob Agents Chemother (2008) 52: 3589-3596 [PMID:18644957] |
| CCR1/C-C chemokine receptor type 1 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL2413] [GtoPdb: 58] [UniProtKB: P32246] | ||||||||
| ChEMBL | Displacement of [125I]-CCL3 from human CCR1 transfected in COS7 cells coexpressing chimeric Gqi4myr after 3 hrs | B | 4.1 | pIC50 | 79432.82 | nM | IC50 | J Med Chem (2012) 55: 8164-8177 [PMID:22957890] |
| ChEMBL | Displacement of [125I]-CCL3 from human CCR1 transfected in COS7 cells coexpressing chimeric Gqi4myr after 3 hrs | B | 4.13 | pIC50 | 74000 | nM | IC50 | J Med Chem (2012) 55: 8164-8177 [PMID:22957890] |
| ChEMBL | Allosteric modulation at human CCR1 transfected in COS7 cells coexpressing chimeric Gqi4myr assessed as {3H]IP3 turnover by liquid scintillation counting analysis | F | 5.2 | pEC50 | 6309.57 | nM | EC50 | J Med Chem (2012) 55: 8164-8177 [PMID:22957890] |
| ChEMBL | Allosteric modulation at human CCR1 transfected in COS7 cells coexpressing chimeric Gqi4myr assessed as {3H]IP3 turnover by liquid scintillation counting analysis | F | 5.23 | pEC50 | 5900 | nM | EC50 | J Med Chem (2012) 55: 8164-8177 [PMID:22957890] |
| CCR5/C-C chemokine receptor type 5 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL274] [GtoPdb: 62] [UniProtKB: P51681] | ||||||||
| ChEMBL | Displacement of [125I]-CCL3 from human CCR5 transfected in COS7 cells coexpressing chimeric Gqi4myr after 3 hrs | B | 4.28 | pIC50 | 53000 | nM | IC50 | J Med Chem (2012) 55: 8164-8177 [PMID:22957890] |
| ChEMBL | Displacement of [125I]-CCL3 from human CCR5 transfected in COS7 cells coexpressing chimeric Gqi4myr after 3 hrs | B | 4.3 | pIC50 | 50118.72 | nM | IC50 | J Med Chem (2012) 55: 8164-8177 [PMID:22957890] |
| ChEMBL | Allosteric modulation at human CCR5 transfected in COS7 cells coexpressing chimeric Gqi4myr assessed as [3H]IP3 turnover by liquid scintillation counting analysis | F | 5.3 | pEC50 | 5011.87 | nM | EC50 | J Med Chem (2012) 55: 8164-8177 [PMID:22957890] |
| ChEMBL | Allosteric modulation at human CCR5 transfected in COS7 cells coexpressing chimeric Gqi4myr assessed as [3H]IP3 turnover by liquid scintillation counting analysis | F | 5.31 | pEC50 | 4900 | nM | EC50 | J Med Chem (2012) 55: 8164-8177 [PMID:22957890] |
| CCR8/C-C chemokine receptor type 8 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4596] [GtoPdb: 65] [UniProtKB: P51685] | ||||||||
| ChEMBL | Allosteric modulation at human CCR8 transfected in COS7 cells assessed as [3H]IP3 turnover by liquid scintillation counting analysis | F | 5.4 | pEC50 | 3981.07 | nM | EC50 | J Med Chem (2012) 55: 8164-8177 [PMID:22957890] |
| ChEMBL | Allosteric modulation at human CCR8 transfected in COS7 cells assessed as [3H]IP3 turnover by liquid scintillation counting analysis | F | 5.41 | pEC50 | 3900 | nM | EC50 | J Med Chem (2012) 55: 8164-8177 [PMID:22957890] |
| Class B carbapenemase VIM-13 in Pseudomonas aeruginosa (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1287600] [UniProtKB: Q2HY42] | ||||||||
| ChEMBL | Inhibition of Pseudomonas aeruginosa VIM-13 beta-lactamase after 10 mins | B | 4.16 | pIC50 | 69300 | nM | IC50 | Antimicrob Agents Chemother (2008) 52: 3589-3596 [PMID:18644957] |
| MMP13/Collagenase 3 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL280] [GtoPdb: 1637] [UniProtKB: P45452] | ||||||||
| ChEMBL | In vitro MMP-8 Assay: The synthetic octapeptide substrate, containing the collagenase-susceptible glycine-isoleucine peptide bond, was incubated (37° C.) with commercially-available chromatrographically-purified human neutrophil collagenase (MMP-8) in the presence of 1 mM Ca++ and the tripeptide degradation fragment and undegraded substrate were separated and measured by HPLC (Waters Alliance 2695 System with a reverse phase C-18 column). | B | 5.4 | pIC50 | 4000 | nM | IC50 | US-9187406-B2. Curcumin analogues as zinc chelators and their uses (2015) |
| ChEMBL | Inhibition of MMPs: It has been observed that 50 and 100 μM concentrations of curcumin decreased TNFα production by endotoxin-stimulated human monocytes (HMs) in culture by 80-90% (lower concentrations of curcumin, 10 and 20 μM, had no effect). However, this inhibitory effect was associated with some precipitation of the curcumin in cell culture and with significant cytotoxicity. It was hypothesized that increasing the solubility of curcumin will: (i) enhance its efficacy as an inhibitor of cytokine expression, (ii) reduce its cytotoxicity, and (iii) preserve (perhaps even enhance; see below) its potency, as an MMP inhibitor (MMPI) compound, which was found to be similar to that of the Zn++ chelating compound, 1,10-O-phenanthroline (FIG. 1). However, it should be noted that excessive inhibition of MMP activity may not be desirable therapeutically because a minimal, or basal, level of MMPs may be necessary for optimal defense of the host. | B | 5.4 | pIC50 | 4000 | nM | IC50 | US-10669227-B2. Curcumin analogues as zinc chelators and their uses (2020) |
| ChEMBL | Inhibition Assay: Table 10: The efficacy of MMP-2 inhibition was as follows: compound 6>compound 7>compound 8. Although compound 6 showed similar efficacy as curcumin when comparing MMP-2 inhibitory potency, the amide-containing compounds are much more soluble than the famously insoluble curcumin. The amide-containing curcumin derivatives are much more potent inhibitors of MMP-13 (Collagenase-3) than curcumin and even more potent than compound 1 (Table 9 and 10).: | B | 5.4 | pIC50 | 4000 | nM | IC50 | US-11608309-B2. Curcumin analogues as zinc chelators and their uses (2023) |
| MMP9/Matrix metalloproteinase-9 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL321] [GtoPdb: 1633] [UniProtKB: P14780] | ||||||||
| ChEMBL | In vitro MMP-8 Assay: The synthetic octapeptide substrate, containing the collagenase-susceptible glycine-isoleucine peptide bond, was incubated (37° C.) with commercially-available chromatrographically-purified human neutrophil collagenase (MMP-8) in the presence of 1 mM Ca++ and the tripeptide degradation fragment and undegraded substrate were separated and measured by HPLC (Waters Alliance 2695 System with a reverse phase C-18 column). | B | 5.05 | pIC50 | 9000 | nM | IC50 | US-9187406-B2. Curcumin analogues as zinc chelators and their uses (2015) |
| ChEMBL | Inhibition of MMPs: It has been observed that 50 and 100 μM concentrations of curcumin decreased TNFα production by endotoxin-stimulated human monocytes (HMs) in culture by 80-90% (lower concentrations of curcumin, 10 and 20 μM, had no effect). However, this inhibitory effect was associated with some precipitation of the curcumin in cell culture and with significant cytotoxicity. It was hypothesized that increasing the solubility of curcumin will: (i) enhance its efficacy as an inhibitor of cytokine expression, (ii) reduce its cytotoxicity, and (iii) preserve (perhaps even enhance; see below) its potency, as an MMP inhibitor (MMPI) compound, which was found to be similar to that of the Zn++ chelating compound, 1,10-O-phenanthroline (FIG. 1). However, it should be noted that excessive inhibition of MMP activity may not be desirable therapeutically because a minimal, or basal, level of MMPs may be necessary for optimal defense of the host. | B | 5.05 | pIC50 | 9000 | nM | IC50 | US-10669227-B2. Curcumin analogues as zinc chelators and their uses (2020) |
| ChEMBL | Inhibition Assay: Table 1 shows the IC50 of curcumin, compound 1, and compound 2, compared to a standard Zn++ binding & MMPI (matrix metalloproteinase inhibitor), 1,10-O-phenanthroline (o-phen), against purified human PMN MMP-8 (from EMD biologics, Inc., Gibbstown, N.J.) using a synthetic octapeptide containing the collagenase-susceptible glycine-isoleucine peptide bond and measuring the tripeptide breakdown products by HPLC (Waters Alliance 2695 System with a reverse phase C-18 column). Compound 1 was an excellent MMPI with an IC50 equivalent to that of 1,10-O-phenanthroline, while compound 2, which lacked substituents on the aryl moieties, did not show a dose response. | B | 5.05 | pIC50 | 9000 | nM | IC50 | US-11608309-B2. Curcumin analogues as zinc chelators and their uses (2023) |
| MMP8/Neutrophil collagenase in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4588] [GtoPdb: 1632] [UniProtKB: P22894] | ||||||||
| ChEMBL | In vitro MMP-8 Assay: The synthetic octapeptide substrate, containing the collagenase-susceptible glycine-isoleucine peptide bond, was incubated (37° C.) with commercially-available chromatrographically-purified human neutrophil collagenase (MMP-8) in the presence of 1 mM Ca++ and the tripeptide degradation fragment and undegraded substrate were separated and measured by HPLC (Waters Alliance 2695 System with a reverse phase C-18 column). | B | 4.46 | pIC50 | 35000 | nM | IC50 | US-9187406-B2. Curcumin analogues as zinc chelators and their uses (2015) |
| ChEMBL | Inhibition of MMPs: It has been observed that 50 and 100 μM concentrations of curcumin decreased TNFα production by endotoxin-stimulated human monocytes (HMs) in culture by 80-90% (lower concentrations of curcumin, 10 and 20 μM, had no effect). However, this inhibitory effect was associated with some precipitation of the curcumin in cell culture and with significant cytotoxicity. It was hypothesized that increasing the solubility of curcumin will: (i) enhance its efficacy as an inhibitor of cytokine expression, (ii) reduce its cytotoxicity, and (iii) preserve (perhaps even enhance; see below) its potency, as an MMP inhibitor (MMPI) compound, which was found to be similar to that of the Zn++ chelating compound, 1,10-O-phenanthroline (FIG. 1). However, it should be noted that excessive inhibition of MMP activity may not be desirable therapeutically because a minimal, or basal, level of MMPs may be necessary for optimal defense of the host. | B | 4.65 | pIC50 | 22500 | nM | IC50 | US-10669227-B2. Curcumin analogues as zinc chelators and their uses (2020) |
| ChEMBL | Inhibition Assay: Table 1 shows the IC50 of curcumin, compound 1, and compound 2, compared to a standard Zn++ binding & MMPI (matrix metalloproteinase inhibitor), 1,10-O-phenanthroline (o-phen), against purified human PMN MMP-8 (from EMD biologics, Inc., Gibbstown, N.J.) using a synthetic octapeptide containing the collagenase-susceptible glycine-isoleucine peptide bond and measuring the tripeptide breakdown products by HPLC (Waters Alliance 2695 System with a reverse phase C-18 column). Compound 1 was an excellent MMPI with an IC50 equivalent to that of 1,10-O-phenanthroline, while compound 2, which lacked substituents on the aryl moieties, did not show a dose response. | B | 4.65 | pIC50 | 22500 | nM | IC50 | US-11608309-B2. Curcumin analogues as zinc chelators and their uses (2023) |
| ChEMBL | In vitro MMP-8 Assay: The synthetic octapeptide substrate, containing the collagenase-susceptible glycine-isoleucine peptide bond, was incubated (37° C.) with commercially-available chromatrographically-purified human neutrophil collagenase (MMP-8) in the presence of 1 mM Ca++ and the tripeptide degradation fragment and undegraded substrate were separated and measured by HPLC (Waters Alliance 2695 System with a reverse phase C-18 column). | B | 5 | pIC50 | 10000 | nM | IC50 | US-9187406-B2. Curcumin analogues as zinc chelators and their uses (2015) |
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]
