lovingscience/chembl-v37-raw-activities huggingface dataset:
Compound (SMILES): FC(F)(F)c1ccc(Cl)c(OC2CCN(c3nccnn3)C2)c1
InChIKey: WWBVCAKAKGRAPT-UHFFFAOYSA-N
Target: Stearoyl-CoA desaturase (SINGLE PROTEIN), Homo sapiens
UniProt: O00767
Assay: Enzyme Inhibition Assay: Human SCD-1 enzyme activity using HepG2 cell microsomes after treating with inhibitory compounds (% inhibition):Human hepatocarcinoma HepG2 cells (ATCC, HB-8065) are cultured to confluence and trypsinised. The cell pellet is taken up with 10 mM Tris (pH 7.4) sucrose (250 mM) DTT (1 mM) buffer and the cells are lysed by sonication. The microsomes are obtained after centrifugation at 10,000 g for 20 minutes at 4 C. followed by centrifugation of the supernatant at 100,000 g for 60 minutes at 4 C. The pellet is taken up with 10 mM Tris (pH 7.4) sucrose (250 mM) buffer at 4 C. and the microsomal proteins are assayed and stored at -196 C. (liquid nitrogen).The enzyme reaction measures the conversion of stearic acid (C18:0 fatty acid) to oleic acid (C18:1 fatty acid) by SCD-1. The enzyme reaction is started by adding 125 ug of HepG2 cell microsomal fraction to tubes (total reaction volume of 500 ul) containing 62 uM of stearic acid.
Measurement: IC50 = 650 nM (pChEMBL 6.190000057220459)
Descriptors: MW 344.72, ALogP 3.2, HBA 5, HBD 0, PSA 51.14, QED 0.86
Compound (SMILES): CCCCCCCCC1=C(CCCCCCCC(=O)O)C1
InChIKey: PQRKPYLNZGDCFH-UHFFFAOYSA-N
Target: Stearoyl-CoA desaturase (SINGLE PROTEIN), Homo sapiens
UniProt: O00767
Assay: Enzyme Inhibition Assay: Human SCD-1 enzyme activity using HepG2 cell microsomes after treating with inhibitory compounds (% inhibition):Human hepatocarcinoma HepG2 cells (ATCC, HB-8065) are cultured to confluence and trypsinised. The cell pellet is taken up with 10 mM Tris (pH 7.4) sucrose (250 mM) DTT (1 mM) buffer and the cells are lysed by sonication. The microsomes are obtained after centrifugation at 10,000 g for 20 minutes at 4 C. followed by centrifugation of the supernatant at 100,000 g for 60 minutes at 4 C. The pellet is taken up with 10 mM Tris (pH 7.4) sucrose (250 mM) buffer at 4 C. and the microsomal proteins are assayed and stored at -196 C. (liquid nitrogen).The enzyme reaction measures the conversion of stearic acid (C18:0 fatty acid) to oleic acid (C18:1 fatty acid) by SCD-1. The enzyme reaction is started by adding 125 ug of HepG2 cell microsomal fraction to tubes (total reaction volume of 500 ul) containing 62 uM of stearic acid.
Measurement: IC50 = 300 nM (pChEMBL 6.519999980926514)
Descriptors: MW 294.48, ALogP 6.25, HBA 1, HBD 1, PSA 37.3, QED 0.29
Compound (SMILES): COc1cc(F)c2c(c1)C1(N=C(N)n3ccnc31)c1cc(-c3cccnc3F)ccc1O2
InChIKey: VNEGKSKZUFSXDG-UHFFFAOYSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: FRET (Fluorescence Resonance Energy Transfer) Assay: The assay buffer used in this screen is 0.05 M acetate, pH 4.2, 10% DMSO final, 100 uM genapol (which is a nonionic detergent, below its Critical Micelle Concentration). The Beta Secretase enzyme (0.2 nM) is pre-incubated for one hour with inhibitors, typically in about 1 uL of DMSO according to a serial dilution, are added thereto. This assay is effectively started by the addition of FRET substrate (50 nM) and the combination is incubated for one hour. The FRET assay is terminated with by addition of Tris buffer, which raises the pH to neutrality, and the fluorescence is determined. The FRET substrate is a peptide with commercially available fluorophore and quencher, on opposite sides of the BACE cleavage site. Proteolytic cleavage of the FRET substrate releases quenching of fluorescence (excitation 488 nm and emission 425 nm).
Measurement: IC50 = 9 nM (pChEMBL 8.050000190734863)
Descriptors: MW 431.4, ALogP 3.81, HBA 7, HBD 1, PSA 87.55, QED 0.49
Compound (SMILES): NC1=N[C@]2(c3cc(-c4cccnc4F)ccc3Oc3c(F)cc(-c4ccnc(F)c4)cc32)c2nccn21
InChIKey: VTTLVOMLUUKPMB-MHZLTWQESA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: FRET (Fluorescence Resonance Energy Transfer) Assay: The assay buffer used in this screen is 0.05 M acetate, pH 4.2, 10% DMSO final, 100 uM genapol (which is a nonionic detergent, below its Critical Micelle Concentration). The Beta Secretase enzyme (0.2 nM) is pre-incubated for one hour with inhibitors, typically in about 1 uL of DMSO according to a serial dilution, are added thereto. This assay is effectively started by the addition of FRET substrate (50 nM) and the combination is incubated for one hour. The FRET assay is terminated with by addition of Tris buffer, which raises the pH to neutrality, and the fluorescence is determined. The FRET substrate is a peptide with commercially available fluorophore and quencher, on opposite sides of the BACE cleavage site. Proteolytic cleavage of the FRET substrate releases quenching of fluorescence (excitation 488 nm and emission 425 nm).
Measurement: IC50 = 10 nM (pChEMBL 8)
Descriptors: MW 496.45, ALogP 5, HBA 7, HBD 1, PSA 91.21, QED 0.35
Compound (SMILES): NC1=N[C@@]2(c3cc(-c4cccnc4F)ccc3Oc3c(F)cc(-c4ccnc(F)c4)cc32)c2nccn21
InChIKey: VTTLVOMLUUKPMB-HHHXNRCGSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: FRET (Fluorescence Resonance Energy Transfer) Assay: The assay buffer used in this screen is 0.05 M acetate, pH 4.2, 10% DMSO final, 100 uM genapol (which is a nonionic detergent, below its Critical Micelle Concentration). The Beta Secretase enzyme (0.2 nM) is pre-incubated for one hour with inhibitors, typically in about 1 uL of DMSO according to a serial dilution, are added thereto. This assay is effectively started by the addition of FRET substrate (50 nM) and the combination is incubated for one hour. The FRET assay is terminated with by addition of Tris buffer, which raises the pH to neutrality, and the fluorescence is determined. The FRET substrate is a peptide with commercially available fluorophore and quencher, on opposite sides of the BACE cleavage site. Proteolytic cleavage of the FRET substrate releases quenching of fluorescence (excitation 488 nm and emission 425 nm).
Measurement: IC50 = 0.3 nM (pChEMBL 9.520000457763672)
Descriptors: MW 496.45, ALogP 5, HBA 7, HBD 1, PSA 91.21, QED 0.35
Compound (SMILES): NC1=N[C@@]2(c3cc(-c4cccnc4F)ccc3Oc3c(F)cc(C4=CCCOC4)cc32)c2nccn21
InChIKey: DQYWRLHJYCHMPT-HHHXNRCGSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: FRET (Fluorescence Resonance Energy Transfer) Assay: The assay buffer used in this screen is 0.05 M acetate, pH 4.2, 10% DMSO final, 100 uM genapol (which is a nonionic detergent, below its Critical Micelle Concentration). The Beta Secretase enzyme (0.2 nM) is pre-incubated for one hour with inhibitors, typically in about 1 uL of DMSO according to a serial dilution, are added thereto. This assay is effectively started by the addition of FRET substrate (50 nM) and the combination is incubated for one hour. The FRET assay is terminated with by addition of Tris buffer, which raises the pH to neutrality, and the fluorescence is determined. The FRET substrate is a peptide with commercially available fluorophore and quencher, on opposite sides of the BACE cleavage site. Proteolytic cleavage of the FRET substrate releases quenching of fluorescence (excitation 488 nm and emission 425 nm).
Measurement: IC50 = 23 nM (pChEMBL 7.639999866485596)
Descriptors: MW 483.48, ALogP 4.6, HBA 7, HBD 1, PSA 87.55, QED 0.42
Compound (SMILES): NC1=N[C@]2(c3cc(-c4cccnc4F)ccc3Oc3c(F)cc(C4=CCCOC4)cc32)c2nccn21
InChIKey: DQYWRLHJYCHMPT-MHZLTWQESA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: FRET (Fluorescence Resonance Energy Transfer) Assay: The assay buffer used in this screen is 0.05 M acetate, pH 4.2, 10% DMSO final, 100 uM genapol (which is a nonionic detergent, below its Critical Micelle Concentration). The Beta Secretase enzyme (0.2 nM) is pre-incubated for one hour with inhibitors, typically in about 1 uL of DMSO according to a serial dilution, are added thereto. This assay is effectively started by the addition of FRET substrate (50 nM) and the combination is incubated for one hour. The FRET assay is terminated with by addition of Tris buffer, which raises the pH to neutrality, and the fluorescence is determined. The FRET substrate is a peptide with commercially available fluorophore and quencher, on opposite sides of the BACE cleavage site. Proteolytic cleavage of the FRET substrate releases quenching of fluorescence (excitation 488 nm and emission 425 nm).
Measurement: IC50 = 0.4 nM (pChEMBL 9.399999618530273)
Descriptors: MW 483.48, ALogP 4.6, HBA 7, HBD 1, PSA 87.55, QED 0.42
Compound (SMILES): Cc1ccc(-c2cc(F)c3c(c2)[C@]2(N=C(N)n4ccnc42)c2cc(-c4cccnc4F)ccc2O3)cc1
InChIKey: ZKCJVDNRTDFWSR-GDLZYMKVSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: FRET (Fluorescence Resonance Energy Transfer) Assay: The assay buffer used in this screen is 0.05 M acetate, pH 4.2, 10% DMSO final, 100 uM genapol (which is a nonionic detergent, below its Critical Micelle Concentration). The Beta Secretase enzyme (0.2 nM) is pre-incubated for one hour with inhibitors, typically in about 1 uL of DMSO according to a serial dilution, are added thereto. This assay is effectively started by the addition of FRET substrate (50 nM) and the combination is incubated for one hour. The FRET assay is terminated with by addition of Tris buffer, which raises the pH to neutrality, and the fluorescence is determined. The FRET substrate is a peptide with commercially available fluorophore and quencher, on opposite sides of the BACE cleavage site. Proteolytic cleavage of the FRET substrate releases quenching of fluorescence (excitation 488 nm and emission 425 nm).
Measurement: IC50 = 114 nM (pChEMBL 6.940000057220459)
Descriptors: MW 491.5, ALogP 5.77, HBA 6, HBD 1, PSA 78.32, QED 0.32
Compound (SMILES): Cc1ccc(-c2cc(F)c3c(c2)[C@@]2(N=C(N)n4ccnc42)c2cc(-c4cccnc4F)ccc2O3)cc1
InChIKey: ZKCJVDNRTDFWSR-LJAQVGFWSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: FRET (Fluorescence Resonance Energy Transfer) Assay: The assay buffer used in this screen is 0.05 M acetate, pH 4.2, 10% DMSO final, 100 uM genapol (which is a nonionic detergent, below its Critical Micelle Concentration). The Beta Secretase enzyme (0.2 nM) is pre-incubated for one hour with inhibitors, typically in about 1 uL of DMSO according to a serial dilution, are added thereto. This assay is effectively started by the addition of FRET substrate (50 nM) and the combination is incubated for one hour. The FRET assay is terminated with by addition of Tris buffer, which raises the pH to neutrality, and the fluorescence is determined. The FRET substrate is a peptide with commercially available fluorophore and quencher, on opposite sides of the BACE cleavage site. Proteolytic cleavage of the FRET substrate releases quenching of fluorescence (excitation 488 nm and emission 425 nm).
Measurement: IC50 = 0.4 nM (pChEMBL 9.399999618530273)
Descriptors: MW 491.5, ALogP 5.77, HBA 6, HBD 1, PSA 78.32, QED 0.32
Compound (SMILES): NC1=N[C@@]2(c3cc(-c4cccnc4F)ccc3Oc3c(F)cc(N4CCOCC4)cc32)c2nccn21
InChIKey: OLMKWMUFWPWVRZ-AREMUKBSSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: FRET (Fluorescence Resonance Energy Transfer) Assay: The assay buffer used in this screen is 0.05 M acetate, pH 4.2, 10% DMSO final, 100 uM genapol (which is a nonionic detergent, below its Critical Micelle Concentration). The Beta Secretase enzyme (0.2 nM) is pre-incubated for one hour with inhibitors, typically in about 1 uL of DMSO according to a serial dilution, are added thereto. This assay is effectively started by the addition of FRET substrate (50 nM) and the combination is incubated for one hour. The FRET assay is terminated with by addition of Tris buffer, which raises the pH to neutrality, and the fluorescence is determined. The FRET substrate is a peptide with commercially available fluorophore and quencher, on opposite sides of the BACE cleavage site. Proteolytic cleavage of the FRET substrate releases quenching of fluorescence (excitation 488 nm and emission 425 nm).
Measurement: IC50 = 0.7 nM (pChEMBL 9.149999618530273)
Descriptors: MW 486.48, ALogP 3.63, HBA 8, HBD 1, PSA 90.79, QED 0.44
Compound (SMILES): NC1=N[C@]2(c3cc(-c4cccnc4F)ccc3Oc3c(F)cc(N4CCOCC4)cc32)c2nccn21
InChIKey: OLMKWMUFWPWVRZ-SANMLTNESA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: FRET (Fluorescence Resonance Energy Transfer) Assay: The assay buffer used in this screen is 0.05 M acetate, pH 4.2, 10% DMSO final, 100 uM genapol (which is a nonionic detergent, below its Critical Micelle Concentration). The Beta Secretase enzyme (0.2 nM) is pre-incubated for one hour with inhibitors, typically in about 1 uL of DMSO according to a serial dilution, are added thereto. This assay is effectively started by the addition of FRET substrate (50 nM) and the combination is incubated for one hour. The FRET assay is terminated with by addition of Tris buffer, which raises the pH to neutrality, and the fluorescence is determined. The FRET substrate is a peptide with commercially available fluorophore and quencher, on opposite sides of the BACE cleavage site. Proteolytic cleavage of the FRET substrate releases quenching of fluorescence (excitation 488 nm and emission 425 nm).
Measurement: IC50 = 189 nM (pChEMBL 6.71999979019165)
Descriptors: MW 486.48, ALogP 3.63, HBA 8, HBD 1, PSA 90.79, QED 0.44
Compound (SMILES): COc1cc(F)c2c(c1)[C@@]1(N=C(N)N3CCCN=C31)c1cc(-c3cccnc3F)ccc1O2
InChIKey: NRCWGDBHISLYPV-DEOSSOPVSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: FRET (Fluorescence Resonance Energy Transfer) Assay: The assay buffer used in this screen is 0.05 M acetate, pH 4.2, 10% DMSO final, 100 uM genapol (which is a nonionic detergent, below its Critical Micelle Concentration). The Beta Secretase enzyme (0.2 nM) is pre-incubated for one hour with inhibitors, typically in about 1 uL of DMSO according to a serial dilution, are added thereto. This assay is effectively started by the addition of FRET substrate (50 nM) and the combination is incubated for one hour. The FRET assay is terminated with by addition of Tris buffer, which raises the pH to neutrality, and the fluorescence is determined. The FRET substrate is a peptide with commercially available fluorophore and quencher, on opposite sides of the BACE cleavage site. Proteolytic cleavage of the FRET substrate releases quenching of fluorescence (excitation 488 nm and emission 425 nm).
Measurement: IC50 = 22 nM (pChEMBL 7.659999847412109)
Descriptors: MW 447.45, ALogP 3.82, HBA 7, HBD 1, PSA 85.33, QED 0.6
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1ccc2nsnc2c1
InChIKey: QNIMPEFZOBTPAU-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 6.07 nM (pChEMBL 8.220000267028809)
Descriptors: MW 350.36, ALogP 2.37, HBA 6, HBD 2, PSA 103.87, QED 0.54
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1ccccc1
InChIKey: HZEIAWPYZBVCBW-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 41.3 nM (pChEMBL 7.380000114440918)
Descriptors: MW 292.3, ALogP 2.36, HBA 3, HBD 2, PSA 78.09, QED 0.71
Compound (SMILES): Cc1ccc(O)c(C2C(=O)NC(=O)N2c2ccc3[nH]cnc3c2)c1
InChIKey: NTNRIUAFBHODRG-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 48 nM (pChEMBL 7.320000171661377)
Descriptors: MW 322.32, ALogP 2.37, HBA 4, HBD 3, PSA 98.32, QED 0.63
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1cc(C(F)(F)F)ccc1F
InChIKey: REJXADCEWQSQLJ-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 51.6 nM (pChEMBL 7.289999961853027)
Descriptors: MW 378.29, ALogP 3.52, HBA 3, HBD 2, PSA 78.09, QED 0.53
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1cc(F)ccc1Br
InChIKey: TXBCOCGENUWIHP-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 34.8 nM (pChEMBL 7.460000038146973)
Descriptors: MW 389.18, ALogP 3.26, HBA 3, HBD 2, PSA 78.09, QED 0.66
Compound (SMILES): CCCOc1ccc(C2C(=O)NC(=O)N2c2ccc3[nH]cnc3c2)cc1
InChIKey: GTFPAKYEYXNXOT-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Binding affinity to QPCT (unknown origin) assessed as inhibition constant
Measurement: Ki = 38 nM (pChEMBL 7.420000076293945)
Descriptors: MW 350.38, ALogP 3.15, HBA 4, HBD 2, PSA 87.32, QED 0.69
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1ccc(Cl)c(C(F)(F)F)c1
InChIKey: MXPHBFZARPUTMB-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 65.5 nM (pChEMBL 7.179999828338623)
Descriptors: MW 394.74, ALogP 4.03, HBA 3, HBD 2, PSA 78.09, QED 0.64
Compound (SMILES): COc1ccc(C2C(=O)NC(=O)N2c2ccc3[nH]cnc3c2)cc1O
InChIKey: JWLPLQZPWGTGDM-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 3.24 nM (pChEMBL 8.489999771118164)
Descriptors: MW 338.32, ALogP 2.07, HBA 5, HBD 3, PSA 107.55, QED 0.63
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1ccc(-c2ccccc2)cc1
InChIKey: HEXVNBQITIFOKU-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 4.13 nM (pChEMBL 8.380000114440918)
Descriptors: MW 368.4, ALogP 4.03, HBA 3, HBD 2, PSA 78.09, QED 0.54
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1cccc(Cl)c1
InChIKey: WADYLOHJJCSTAF-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 36 nM (pChEMBL 7.440000057220459)
Descriptors: MW 326.74, ALogP 3.01, HBA 3, HBD 2, PSA 78.09, QED 0.71
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1ccc(Cl)cc1
InChIKey: ROKHRVRZZBNKGJ-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 42.8 nM (pChEMBL 7.369999885559082)
Descriptors: MW 326.74, ALogP 3.01, HBA 3, HBD 2, PSA 78.09, QED 0.71
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1ccccc1Cl
InChIKey: PHTVQKCBKDWZBY-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 21.7 nM (pChEMBL 7.659999847412109)
Descriptors: MW 326.74, ALogP 3.01, HBA 3, HBD 2, PSA 78.09, QED 0.71
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1ccc(F)cc1
InChIKey: CEZNAXCARYIAEU-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 58.5 nM (pChEMBL 7.230000019073486)
Descriptors: MW 310.29, ALogP 2.5, HBA 3, HBD 2, PSA 78.09, QED 0.71
Compound (SMILES): O=C1NC(=O)N(c2ccc3[nH]cnc3c2)C1c1ccc2c(c1)OCCO2
InChIKey: AJUGSLXCFBLQHE-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 13.6 nM (pChEMBL 7.869999885559082)
Descriptors: MW 350.33, ALogP 2.13, HBA 5, HBD 2, PSA 96.55, QED 0.69
Compound (SMILES): O=C1NC(=O)C2(Cc3ccccc3C2)N1c1ccc2[nH]cnc2c1
InChIKey: SOCSUCKHKHAOMU-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 159 nM (pChEMBL 6.800000190734863)
Descriptors: MW 318.34, ALogP 2.16, HBA 3, HBD 2, PSA 78.09, QED 0.67
Compound (SMILES): O=C1NC(=S)C(c2ccc(Cl)cc2)N1c1ccc2[nH]cnc2c1
InChIKey: XPTXSMOWEGMJQC-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 45.9 nM (pChEMBL 7.340000152587891)
Descriptors: MW 342.81, ALogP 3.81, HBA 3, HBD 2, PSA 61.02, QED 0.7
Compound (SMILES): O=C1NC(=S)C(c2ccc(F)c(F)c2F)N1c1ccc2nc[nH]c2c1
InChIKey: NGJZDGZTGWZQHU-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 85.3 nM (pChEMBL 7.070000171661377)
Descriptors: MW 362.34, ALogP 3.58, HBA 3, HBD 2, PSA 61.02, QED 0.54
Compound (SMILES): O=C1NC(=S)C(c2ccc(Br)cc2F)N1c1ccc2nc[nH]c2c1
InChIKey: CVLWWSXQLNSNGF-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 6.49 nM (pChEMBL 8.1899995803833)
Descriptors: MW 405.25, ALogP 4.06, HBA 3, HBD 2, PSA 61.02, QED 0.63
Compound (SMILES): Cc1ccc(C2C(=S)NC(=O)N2c2ccc3[nH]cnc3c2)c(F)c1F
InChIKey: AZZFRDKXGUGTRC-UHFFFAOYSA-N
Target: Glutaminyl-peptide cyclotransferase (SINGLE PROTEIN), Homo sapiens
UniProt: Q16769
Assay: Spectrophotometric Assay: This novel assay was used to determine the kinetic parameters for most of the QC substrates. QC activity was analyzed spectrophotometrically using a continuous method, that was derived by adapting a previous discontinuous assay (Bateman, R. C. J. 1989 J Neurosci Methods 30, 23-28) utilizing glutamate dehydrogenase as auxiliary enzyme. Samples consisted of the respective QC substrate, 0.3 mM NADH, 14 mM alpha-Ketoglutaric acid and 30 U/ml glutamate dehydrogenase in a final volume of 250 ul. Reactions were started by addition of QC and persued by monitoring of the decrease in absorbance at 340 nm for 8-15 min. The initial velocities were evaluated and the enzymatic activity was determined from a standard curve of ammonia under assay conditions. All samples were measured at 30 C., using either the SPECTRAFluor Plus or the Sunrise (both from TECAN) reader for microplates. Kinetic data was evaluated using GraFit software.
Measurement: Ki = 17.7 nM (pChEMBL 7.75)
Descriptors: MW 358.37, ALogP 3.75, HBA 3, HBD 2, PSA 61.02, QED 0.69
Compound (SMILES): CC(C)(C)c1ccc2c(c1)CC[C@H]2NC(=O)Nc1cccc2scnc12
InChIKey: YQUGMLHOSTWCGM-MRXNPFEDSA-N
Target: Transient receptor potential cation channel subfamily V member 1 (SINGLE PROTEIN), Homo sapiens
UniProt: Q8NER1
Assay: Activation Assay: The functional activity of compounds at the TRPV1 receptor was determined by measurement of intracellular Ca2+ levels ([Ca2]i) using the Fluorescence Imaging Plate Reader (FLIPR)TETRA. All compounds were tested over a 12-point one-third-log concentration range. Compound stocks, 10 mM, were prepared in DMSO, and diluted serially across a 384-well plate using a Bravo BenchCel workstation (Agilent Technologies, Santa Clara, Calif.). A stock concentration of capsaicin (10 mM) was made in DMSO, and diluted in D-PBS to a final concentration of 200 nM (4x). On the day prior to the experiment, recombinant HEK293 cells that stably express either human or rat TRPV1 (hTRPV1-3) were removed from tissue culture flasks and plated in growth medium into black-walled clear-bottom 384-well Biocoat poly-D-lysine assay plates (BD Biosciences, Bedford, Mass.) using a Multidrop dispenser (ThermoScientific, Waltham, Mass.). On the day of the experiment, growth medium was removed.
Measurement: IC50 = 35 nM (pChEMBL 7.460000038146973)
Descriptors: MW 365.5, ALogP 5.4, HBA 3, HBD 2, PSA 54.02, QED 0.64
Compound (SMILES): CN1C(=O)NCc2c(NC(=O)N[C@@H]3CC(C)(C)Oc4cc(F)ccc43)cccc21
InChIKey: FRGARLJSQHDLGK-MRXNPFEDSA-N
Target: Transient receptor potential cation channel subfamily V member 1 (SINGLE PROTEIN), Homo sapiens
UniProt: Q8NER1
Assay: Activation Assay: The cDNA for human TRPV1 (hTRPV1) was isolated by reverse transcriptase-polymerase chain reaction (RT-PCR) from human small intestine poly A+ RNA supplied by Clontech (Palo Alto, Calif.) using primers designed surrounding the initiation and termination codons identical to the published sequences (Hayes et al. Pain 2000, 88, 205-215). The resulting cDNA PCR products were subcloned into pCIneo mammalian expression vector (Promega) and fully sequenced using fluorescent dye-terminator reagents (Prism, PerkinElmer Applied Biosystems Division) and a PerkinElmer Applied Biosystems Model 373 DNA sequencer or Model 310 genetic analyzer. Expression plasmids encoding the hTRPV1 cDNA were transfected into HEK293 cells using Lipofectamine. Forty-eight hours after transfection, the neomycin-resistant cells were selected with growth medium containing 800 ug/mL Geneticin (Life Technologies, formerly Gibco BRL). Surviving individual colonies were isolated and screened for TRPV1 activity.
Measurement: IC50 = 10 nM (pChEMBL 8)
Descriptors: MW 398.44, ALogP 3.91, HBA 3, HBD 3, PSA 82.7, QED 0.72
Compound (SMILES): CN1C(=O)NCc2c(NC(=O)N[C@@H]3CC(CF)(CF)Oc4cc(Cl)ccc43)cccc21
InChIKey: JFJWXFXLCYCYSG-MRXNPFEDSA-N
Target: Transient receptor potential cation channel subfamily V member 1 (SINGLE PROTEIN), Homo sapiens
UniProt: Q8NER1
Assay: Activation Assay: The cDNA for human TRPV1 (hTRPV1) was isolated by reverse transcriptase-polymerase chain reaction (RT-PCR) from human small intestine poly A+ RNA supplied by Clontech (Palo Alto, Calif.) using primers designed surrounding the initiation and termination codons identical to the published sequences (Hayes et al. Pain 2000, 88, 205-215). The resulting cDNA PCR products were subcloned into pCIneo mammalian expression vector (Promega) and fully sequenced using fluorescent dye-terminator reagents (Prism, PerkinElmer Applied Biosystems Division) and a PerkinElmer Applied Biosystems Model 373 DNA sequencer or Model 310 genetic analyzer. Expression plasmids encoding the hTRPV1 cDNA were transfected into HEK293 cells using Lipofectamine. Forty-eight hours after transfection, the neomycin-resistant cells were selected with growth medium containing 800 ug/mL Geneticin (Life Technologies, formerly Gibco BRL). Surviving individual colonies were isolated and screened for TRPV1 activity.
Measurement: IC50 = 36 nM (pChEMBL 7.440000057220459)
Descriptors: MW 450.87, ALogP 4.32, HBA 3, HBD 3, PSA 82.7, QED 0.65
Compound (SMILES): CN1C(=O)NCc2c(NC(=O)N[C@@H]3CC(CF)(CF)Oc4c3ccc(Cl)c4F)cccc21
InChIKey: FVYLBWIKUIGTIG-OAHLLOKOSA-N
Target: Transient receptor potential cation channel subfamily V member 1 (SINGLE PROTEIN), Homo sapiens
UniProt: Q8NER1
Assay: Activation Assay: The cDNA for human TRPV1 (hTRPV1) was isolated by reverse transcriptase-polymerase chain reaction (RT-PCR) from human small intestine poly A+ RNA supplied by Clontech (Palo Alto, Calif.) using primers designed surrounding the initiation and termination codons identical to the published sequences (Hayes et al. Pain 2000, 88, 205-215). The resulting cDNA PCR products were subcloned into pCIneo mammalian expression vector (Promega) and fully sequenced using fluorescent dye-terminator reagents (Prism, PerkinElmer Applied Biosystems Division) and a PerkinElmer Applied Biosystems Model 373 DNA sequencer or Model 310 genetic analyzer. Expression plasmids encoding the hTRPV1 cDNA were transfected into HEK293 cells using Lipofectamine. Forty-eight hours after transfection, the neomycin-resistant cells were selected with growth medium containing 800 ug/mL Geneticin (Life Technologies, formerly Gibco BRL). Surviving individual colonies were isolated and screened for TRPV1 activity.
Measurement: IC50 = 25 nM (pChEMBL 7.599999904632568)
Descriptors: MW 468.86, ALogP 4.46, HBA 3, HBD 3, PSA 82.7, QED 0.62
Compound (SMILES): CN1C(=O)NCc2c(NC(=O)N[C@@H]3CC(C)(C)Oc4ccccc43)cccc21
InChIKey: XYEJCDHPTOELBI-MRXNPFEDSA-N
Target: Transient receptor potential cation channel subfamily V member 1 (SINGLE PROTEIN), Homo sapiens
UniProt: Q8NER1
Assay: Activation Assay: The cDNA for human TRPV1 (hTRPV1) was isolated by reverse transcriptase-polymerase chain reaction (RT-PCR) from human small intestine poly A+ RNA supplied by Clontech (Palo Alto, Calif.) using primers designed surrounding the initiation and termination codons identical to the published sequences (Hayes et al. Pain 2000, 88, 205-215). The resulting cDNA PCR products were subcloned into pCIneo mammalian expression vector (Promega) and fully sequenced using fluorescent dye-terminator reagents (Prism, PerkinElmer Applied Biosystems Division) and a PerkinElmer Applied Biosystems Model 373 DNA sequencer or Model 310 genetic analyzer. Expression plasmids encoding the hTRPV1 cDNA were transfected into HEK293 cells using Lipofectamine. Forty-eight hours after transfection, the neomycin-resistant cells were selected with growth medium containing 800 ug/mL Geneticin (Life Technologies, formerly Gibco BRL). Surviving individual colonies were isolated and screened for TRPV1 activity.
Measurement: IC50 = 37 nM (pChEMBL 7.429999828338623)
Descriptors: MW 380.45, ALogP 3.77, HBA 3, HBD 3, PSA 82.7, QED 0.74
Compound (SMILES): CN1C(=O)NCc2c(NC(=O)N[C@@H]3CC(C)(C)Oc4c3ccc(F)c4Cl)cccc21
InChIKey: NUCUWBXOAMCKQE-OAHLLOKOSA-N
Target: Transient receptor potential cation channel subfamily V member 1 (SINGLE PROTEIN), Homo sapiens
UniProt: Q8NER1
Assay: Activation Assay: The cDNA for human TRPV1 (hTRPV1) was isolated by reverse transcriptase-polymerase chain reaction (RT-PCR) from human small intestine poly A+ RNA supplied by Clontech (Palo Alto, Calif.) using primers designed surrounding the initiation and termination codons identical to the published sequences (Hayes et al. Pain 2000, 88, 205-215). The resulting cDNA PCR products were subcloned into pCIneo mammalian expression vector (Promega) and fully sequenced using fluorescent dye-terminator reagents (Prism, PerkinElmer Applied Biosystems Division) and a PerkinElmer Applied Biosystems Model 373 DNA sequencer or Model 310 genetic analyzer. Expression plasmids encoding the hTRPV1 cDNA were transfected into HEK293 cells using Lipofectamine. Forty-eight hours after transfection, the neomycin-resistant cells were selected with growth medium containing 800 ug/mL Geneticin (Life Technologies, formerly Gibco BRL). Surviving individual colonies were isolated and screened for TRPV1 activity.
Measurement: IC50 = 17 nM (pChEMBL 7.769999980926514)
Descriptors: MW 432.88, ALogP 4.56, HBA 3, HBD 3, PSA 82.7, QED 0.65
Compound (SMILES): CN1C(=O)NCc2c(NC(=O)N[C@@H]3CC(C)(C)Oc4cc(Cl)ccc43)cccc21
InChIKey: OZDVMEWSDVYDEW-MRXNPFEDSA-N
Target: Transient receptor potential cation channel subfamily V member 1 (SINGLE PROTEIN), Homo sapiens
UniProt: Q8NER1
Assay: Activation Assay: The cDNA for human TRPV1 (hTRPV1) was isolated by reverse transcriptase-polymerase chain reaction (RT-PCR) from human small intestine poly A+ RNA supplied by Clontech (Palo Alto, Calif.) using primers designed surrounding the initiation and termination codons identical to the published sequences (Hayes et al. Pain 2000, 88, 205-215). The resulting cDNA PCR products were subcloned into pCIneo mammalian expression vector (Promega) and fully sequenced using fluorescent dye-terminator reagents (Prism, PerkinElmer Applied Biosystems Division) and a PerkinElmer Applied Biosystems Model 373 DNA sequencer or Model 310 genetic analyzer. Expression plasmids encoding the hTRPV1 cDNA were transfected into HEK293 cells using Lipofectamine. Forty-eight hours after transfection, the neomycin-resistant cells were selected with growth medium containing 800 ug/mL Geneticin (Life Technologies, formerly Gibco BRL). Surviving individual colonies were isolated and screened for TRPV1 activity.
Measurement: IC50 = 42 nM (pChEMBL 7.380000114440918)
Descriptors: MW 414.89, ALogP 4.42, HBA 3, HBD 3, PSA 82.7, QED 0.68