lovingscience/chembl-v37-raw-activities huggingface dataset:
Compound (SMILES): COc1cc(C)c(S(=O)(=O)Nc2cccnc2C)c(C)c1C
InChIKey: GSUHCRFFRPIAJP-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P30419
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 70000 nM (pChEMBL 4.159999847412109)
Descriptors: MW 320.41, ALogP 3.12, HBA 4, HBD 1, PSA 68.29, QED 0.94
Compound (SMILES): CC(C)OC(=O)N1CCC(Oc2cc(Nc3ccc(S(C)(=O)=O)nc3[N+](=O)[O-])ncn2)CC1
InChIKey: PVCFBCABNZROKN-UHFFFAOYSA-N
Target: Glucose-dependent insulinotropic receptor (SINGLE PROTEIN), Rattus norvegicus
UniProt: Q7TQN8
Assay: Agonist activity at rat GPR119 receptor assessed as cAMP production by HTRF assay
Measurement: EC50 > 5000 nM (pChEMBL 5.301000118255615)
Descriptors: MW 480.5, ALogP 2.32, HBA 11, HBD 1, PSA 166.75, QED 0.46
Compound (SMILES): CCCCc1nc(C)c(CC(=S)N(C)C)c(=O)n1Cc1ccc(-c2ccccc2-c2nnn[nH]2)cc1
InChIKey: AMEROGPZOLAFBN-UHFFFAOYSA-N
Target: Type-1 angiotensin II receptor (SINGLE PROTEIN), Homo sapiens
UniProt: P30556
Assay: Antagonist activity at type-1 angiotensin 2 receptor (unknown origin) by calcium mobilizing assay
Measurement: IC50 = 4.5 nM (pChEMBL 8.350000381469727)
Descriptors: MW 501.66, ALogP 4.22, HBA 7, HBD 1, PSA 92.59, QED 0.34
Compound (SMILES): O=C(O)C1CN(Cc2cc(-c3noc(-c4cc(-c5ccccc5)c(C(F)(F)F)s4)n3)cs2)C1
InChIKey: YGTRMKPDETWCJF-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 = 800 nM (pChEMBL 6.099999904632568)
Descriptors: MW 491.52, ALogP 5.73, HBA 7, HBD 1, PSA 79.46, QED 0.37
Compound (SMILES): O=C(O)C1CN(Cc2cc(-c3noc(-c4cccc(-c5ccccc5)c4)n3)cs2)C1
InChIKey: SZZQKFTYGGYXLS-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 > 20000 nM (pChEMBL 4.698999881744385)
Descriptors: MW 417.49, ALogP 4.65, HBA 6, HBD 1, PSA 79.46, QED 0.49
Compound (SMILES): O=C(O)C1CN(Cc2cc(-c3noc(-c4ccc(-c5ccccc5)cc4)n3)cs2)C1
InChIKey: JDZHYDQGMHKABI-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 > 20000 nM (pChEMBL 4.698999881744385)
Descriptors: MW 417.49, ALogP 4.65, HBA 6, HBD 1, PSA 79.46, QED 0.49
Compound (SMILES): O=C(O)C1CN(Cc2cc(-c3noc(-c4ccc(OCc5ccccc5)cc4)n3)cs2)C1
InChIKey: XSVCVRMNJKLDBH-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 > 20000 nM (pChEMBL 4.698999881744385)
Descriptors: MW 447.52, ALogP 4.56, HBA 7, HBD 1, PSA 88.69, QED 0.42
Compound (SMILES): CCCOc1ccc(-c2nc(-c3csc(CN4CC(C(=O)O)C4)c3)no2)cc1
InChIKey: KFIHHKRIJGMXKU-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 > 20000 nM (pChEMBL 4.698999881744385)
Descriptors: MW 399.47, ALogP 3.77, HBA 7, HBD 1, PSA 88.69, QED 0.62
Compound (SMILES): O=C(O)C1CN(Cc2cc(-c3noc(-c4ccc(Oc5ccccc5)cc4)n3)cs2)C1
InChIKey: BBKPNEUTSVSQSU-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 = 4600 nM (pChEMBL 5.340000152587891)
Descriptors: MW 433.49, ALogP 4.77, HBA 7, HBD 1, PSA 88.69, QED 0.45
Compound (SMILES): O=C(O)C1CN(Cc2csc(-c3noc(-c4ccc(Oc5ccccc5)cc4)n3)c2)C1
InChIKey: JIKNJWSBMCSIFA-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 > 20000 nM (pChEMBL 4.698999881744385)
Descriptors: MW 433.49, ALogP 4.77, HBA 7, HBD 1, PSA 88.69, QED 0.45
Compound (SMILES): O=C(O)C1CN(Cc2ccc(-c3noc(-c4ccc(Oc5ccccc5)cc4)n3)s2)C1
InChIKey: OHLZFMQAPXBXJP-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 = 900 nM (pChEMBL 6.050000190734863)
Descriptors: MW 433.49, ALogP 4.77, HBA 7, HBD 1, PSA 88.69, QED 0.45
Compound (SMILES): Cc1ccc(Oc2ccc(-c3nc(-c4csc(CN5CC(C(=O)O)C5)c4)no3)cc2)cc1
InChIKey: YXNTWLJNIOAUDP-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 = 12000 nM (pChEMBL 4.920000076293945)
Descriptors: MW 447.52, ALogP 5.08, HBA 7, HBD 1, PSA 88.69, QED 0.42
Compound (SMILES): Cc1cccc(Oc2ccc(-c3nc(-c4csc(CN5CC(C(=O)O)C5)c4)no3)cc2)c1
InChIKey: GIHPQDVYSVBQIQ-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 > 20000 nM (pChEMBL 4.698999881744385)
Descriptors: MW 447.52, ALogP 5.08, HBA 7, HBD 1, PSA 88.69, QED 0.42
Compound (SMILES): Cc1ccccc1Oc1ccc(-c2nc(-c3csc(CN4CC(C(=O)O)C4)c3)no2)cc1
InChIKey: WZSIVTSIPOTKIW-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 = 2000 nM (pChEMBL 5.699999809265137)
Descriptors: MW 447.52, ALogP 5.08, HBA 7, HBD 1, PSA 88.69, QED 0.42
Compound (SMILES): Cc1cc(-c2nc(-c3csc(CN4CC(C(=O)O)C4)c3)no2)ccc1Oc1ccccc1
InChIKey: UICOPSLHFMXOQP-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 = 3000 nM (pChEMBL 5.519999980926514)
Descriptors: MW 447.52, ALogP 5.08, HBA 7, HBD 1, PSA 88.69, QED 0.42
Compound (SMILES): Cc1cc(Oc2ccccc2)ccc1-c1nc(-c2csc(CN3CC(C(=O)O)C3)c2)no1
InChIKey: UFWYQCXPPYIWBY-UHFFFAOYSA-N
Target: Sphingosine 1-phosphate receptor 3 (SINGLE PROTEIN), Homo sapiens
UniProt: Q99500
Assay: Agonist activity at human S1P3 receptor assessed as stimulation of [35S]GTPgamma binding
Measurement: EC50 > 20000 nM (pChEMBL 4.698999881744385)
Descriptors: MW 447.52, ALogP 5.08, HBA 7, HBD 1, PSA 88.69, QED 0.42
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)Nc2ccccc2)cc1NC(C)=O
InChIKey: LJZJFOIFDKKIFD-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 20000 nM (pChEMBL 4.699999809265137)
Descriptors: MW 350.4, ALogP 2.46, HBA 5, HBD 2, PSA 93.73, QED 0.83
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)N(C)c2ccccc2)cc1NC(C)=O
InChIKey: VLBXOYVWEBHPSO-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 3000 nM (pChEMBL 5.519999980926514)
Descriptors: MW 364.42, ALogP 2.49, HBA 5, HBD 1, PSA 84.94, QED 0.85
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)N(c2ccccc2)C(C)C)cc1NC(C)=O
InChIKey: VHHGJSMODFCCFA-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 2000 nM (pChEMBL 5.699999809265137)
Descriptors: MW 392.48, ALogP 3.27, HBA 5, HBD 1, PSA 84.94, QED 0.78
Compound (SMILES): CCN(c1ccccc1C)S(=O)(=O)c1cc(NC(C)=O)c(OC)cc1OC
InChIKey: IRVGIJWUGUOMCY-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 15000 nM (pChEMBL 4.820000171661377)
Descriptors: MW 392.48, ALogP 3.19, HBA 5, HBD 1, PSA 84.94, QED 0.78
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)N2CCCCC2)cc1NC(C)=O
InChIKey: JDLLUMDTJJUSNT-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 80000 nM (pChEMBL 4.099999904632568)
Descriptors: MW 342.42, ALogP 1.84, HBA 5, HBD 1, PSA 84.94, QED 0.88
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)Nc2ccc(F)cc2)cc1NC(C)=O
InChIKey: PTFAPRDGLWOAMV-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 25000 nM (pChEMBL 4.599999904632568)
Descriptors: MW 368.39, ALogP 2.6, HBA 5, HBD 2, PSA 93.73, QED 0.82
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)Nc2cccc(F)c2)cc1NC(C)=O
InChIKey: SQXTUEAJBJWCIL-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 15000 nM (pChEMBL 4.820000171661377)
Descriptors: MW 368.39, ALogP 2.6, HBA 5, HBD 2, PSA 93.73, QED 0.82
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)Nc2ccccc2F)cc1NC(C)=O
InChIKey: BZJKDIURKBPHOU-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 5000 nM (pChEMBL 5.300000190734863)
Descriptors: MW 368.39, ALogP 2.6, HBA 5, HBD 2, PSA 93.73, QED 0.82
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)Nc2cccc(C)c2)cc1NC(C)=O
InChIKey: MLLRFFQEQMMVCQ-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 17000 nM (pChEMBL 4.769999980926514)
Descriptors: MW 364.42, ALogP 2.77, HBA 5, HBD 2, PSA 93.73, QED 0.82
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)Nc2ccc(C)cc2)cc1NC(C)=O
InChIKey: QLTMJCFLTYHLPY-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 21000 nM (pChEMBL 4.679999828338623)
Descriptors: MW 364.42, ALogP 2.77, HBA 5, HBD 2, PSA 93.73, QED 0.82
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)NCc2ccccc2Br)cc1NC(C)=O
InChIKey: HEIRPWORKWJGJB-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 4000 nM (pChEMBL 5.400000095367432)
Descriptors: MW 443.32, ALogP 2.9, HBA 5, HBD 2, PSA 93.73, QED 0.69
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)NCc2ccccc2N2CCC(CO)CC2)cc1NC(C)=O
InChIKey: RILUGKNQULOTLJ-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 39994.47 nM (pChEMBL 4.400000095367432)
Descriptors: MW 477.58, ALogP 2.35, HBA 7, HBD 3, PSA 117.2, QED 0.51
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)NCc2ccccc2N2CCCCC2)cc1NC(=O)CCC(=O)O
InChIKey: PXTMNXYTOSYHIH-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 2999.16 nM (pChEMBL 5.519999980926514)
Descriptors: MW 505.59, ALogP 2.98, HBA 7, HBD 3, PSA 134.27, QED 0.42
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)NCc2ccccc2N2CCC(CO)CC2)cc1NC(=O)CCC(=O)O
InChIKey: XXSUTSODZMQCST-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 2999.16 nM (pChEMBL 5.519999980926514)
Descriptors: MW 535.62, ALogP 2.19, HBA 8, HBD 4, PSA 154.5, QED 0.32
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)NCc2ccccc2N2CCC(COC(=O)CCC(=O)O)CC2)cc1NC(=O)CCC(=O)O
InChIKey: PRDHHOYRFMTLDT-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 250.03 nM (pChEMBL 6.599999904632568)
Descriptors: MW 635.69, ALogP 2.61, HBA 10, HBD 4, PSA 197.87, QED 0.2
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)NCc2ccccc2-c2ccc(C(=O)O)cc2)cc1NC(=O)CCC(=O)O
InChIKey: ZJOBJQWOISSDKX-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 899.5 nM (pChEMBL 6.050000190734863)
Descriptors: MW 542.57, ALogP 3.35, HBA 7, HBD 4, PSA 168.33, QED 0.27
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)NCc2ccccc2N2CCC(C(=O)O)CC2)cc1NC(=O)CCC(=O)O
InChIKey: HCHWOLFSXYTCQR-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 500.03 nM (pChEMBL 6.300000190734863)
Descriptors: MW 549.6, ALogP 2.29, HBA 8, HBD 4, PSA 171.57, QED 0.31
Compound (SMILES): COc1cc(OC)c(S(=O)(=O)NCc2ccccc2N2CCC(CC(=O)O)CC2)cc1NC(=O)CCC(=O)O
InChIKey: BMIKOSBWXPCSLE-UHFFFAOYSA-N
Target: Bifunctional protein GlmU (SINGLE PROTEIN), Escherichia coli (strain K12)
UniProt: P0ACC7
Assay: Inhibition of Escherichia coli GlmU acetyltransferase activity assessed as coenzyme A production using acetyl CoA substrate
Measurement: IC50 = 399.94 nM (pChEMBL 6.400000095367432)
Descriptors: MW 563.63, ALogP 2.68, HBA 8, HBD 4, PSA 171.57, QED 0.28
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1c(Cl)cc(Br)cc1Cl
InChIKey: SXCJBRNVTQTKSN-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 550 nM (pChEMBL 6.260000228881836)
Descriptors: MW 413.12, ALogP 3.91, HBA 4, HBD 1, PSA 63.99, QED 0.83
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(Cl)nc1
InChIKey: BOEMFNBZIJZNDQ-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 17000 nM (pChEMBL 4.769999980926514)
Descriptors: MW 300.77, ALogP 1.89, HBA 5, HBD 1, PSA 76.88, QED 0.88
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCc2ccccc2)nc1
InChIKey: BFFGKPWVEMOHKA-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 1400 nM (pChEMBL 5.849999904632568)
Descriptors: MW 371.47, ALogP 2.84, HBA 6, HBD 2, PSA 88.91, QED 0.7
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCc2ccc3[nH]ccc3c2)nc1
InChIKey: FPNUWKJFVUJULR-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 340 nM (pChEMBL 6.46999979019165)
Descriptors: MW 410.5, ALogP 3.33, HBA 6, HBD 3, PSA 104.7, QED 0.45
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCCN2CCN(C)CC2)nc1
InChIKey: RLKMGPCSKXTKNK-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 140 nM (pChEMBL 6.849999904632568)
Descriptors: MW 407.54, ALogP 0.89, HBA 8, HBD 2, PSA 95.39, QED 0.7
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCCN2CCNCC2)nc1
InChIKey: QPTPQJCHFTYWMD-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 870 nM (pChEMBL 6.059999942779541)
Descriptors: MW 393.52, ALogP 0.55, HBA 8, HBD 3, PSA 104.18, QED 0.63
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCCN2CCCCC2)nc1
InChIKey: KSTANGOMVMSRPG-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 11200 nM (pChEMBL 4.949999809265137)
Descriptors: MW 392.53, ALogP 2.13, HBA 7, HBD 2, PSA 92.15, QED 0.75
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCCN2CCN(C(C)C)CC2)nc1
InChIKey: GPACLUXKWVKLOA-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 1000 nM (pChEMBL 6)
Descriptors: MW 435.6, ALogP 1.67, HBA 8, HBD 2, PSA 95.39, QED 0.65
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCCC2CCN(C)CC2)nc1
InChIKey: ZLYXHAOYNACFLW-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 30 nM (pChEMBL 7.519999980926514)
Descriptors: MW 406.56, ALogP 2.38, HBA 7, HBD 2, PSA 92.15, QED 0.73
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCCN2CCN(c3ccccc3)CC2)nc1
InChIKey: IIXRYDSDAGBOCO-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 1000 nM (pChEMBL 6)
Descriptors: MW 469.62, ALogP 2.47, HBA 8, HBD 2, PSA 95.39, QED 0.52
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCCCN2CCN(C)CC2)nc1
InChIKey: VCBSTZQLEZNXPL-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 120 nM (pChEMBL 6.920000076293945)
Descriptors: MW 421.57, ALogP 1.28, HBA 8, HBD 2, PSA 95.39, QED 0.62
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCCCn2ccnc2)nc1
InChIKey: CDCHGPKFJGINHS-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 2000 nM (pChEMBL 5.699999809265137)
Descriptors: MW 389.49, ALogP 1.93, HBA 8, HBD 2, PSA 106.73, QED 0.57
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(N2CCC(N3CCNCC3)C2)nc1
InChIKey: DFZWNVAGAJNFJX-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 110 nM (pChEMBL 6.960000038146973)
Descriptors: MW 419.56, ALogP 0.72, HBA 8, HBD 2, PSA 95.39, QED 0.74
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(N2CCCC(N3CCNCC3)C2)nc1
InChIKey: DYBVVKGMMMWRHW-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 3 nM (pChEMBL 8.520000457763672)
Descriptors: MW 433.58, ALogP 1.11, HBA 8, HBD 2, PSA 95.39, QED 0.73
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCCN2CCN(Cc3ccccc3)CC2)nc1
InChIKey: KQEWNJJXOMIHRI-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 10000 nM (pChEMBL 5)
Descriptors: MW 483.64, ALogP 2.46, HBA 8, HBD 2, PSA 95.39, QED 0.48
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1ccc(NCCN2CCN(C(=O)OC(C)(C)C)CC2)nc1
InChIKey: RQEZFBXIHXGHMN-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase (SINGLE PROTEIN), Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
UniProt: Q388H8
Assay: Enzyme Inhibition Assay: Measurements were performed using a modification of the scintillation proximity assay platform described previously by Georgopapadakou, N. H. et al. (22nd International Congress on Chemotherapy, 2001, Abstract P16.001). Compounds were solubilised in DMSO at a top concentration of 10 mM and serially diluted in half log steps to achieve a range of final assay concentrations of 100 uM to 1 nM. Compound at each concentration (100-fold final) was added to white 384 well plates in a volume of 0.5 ml. Human, A. fumigatus, T. brucei or L. major N-myristoyl transferase enzyme, dissolved to a working concentration of 10 nM in assay buffer (30 mM Tris/HCl pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1.25 mM DTT, 0.1% Triton X-100), was then added to columns 1 to 11 and 13 to 23 of the plates in a volume of 20 ml. To columns 12 and 24, 20 ml assay buffer was added to provide a no enzyme control. Following a 5 minute incubation at room temperature the substrates (GCGGSKVKPQPPQAK(Biotin)-Amide and myristoyl coenzyme A), dissolved in assay buffer, were added to all wells in a volume of 20 ml to start the reaction. The final concentrations of peptide and 3H-myristoyl coenzyme A were 0.5 mM and 125 nM respectively and the specific activity of the radiolabel was 8 Ci/mmol. Plates were then incubated at room temperature for up to 50 minutes (dependant upon the period of linearity for the different enzyme species) before SPA beads, suspended to 1 mg/ml in a stop solution (200 mM Phosphoric Acid/NaOH pH 4, 750 mM MgCl2), were added in a volume of 40 ml.
Measurement: IC50 = 1000 nM (pChEMBL 6)
Descriptors: MW 493.63, ALogP 2.2, HBA 9, HBD 2, PSA 121.69, QED 0.6
Compound (SMILES): Cc1nn(C)c(C)c1NS(=O)(=O)c1c(Cl)cc(-c2cccc3cnccc23)cc1Cl
InChIKey: VRGIRQGXJQIDQS-UHFFFAOYSA-N
Target: Glycylpeptide N-tetradecanoyltransferase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P30419
Assay: Inhibition of human N-myristoyltransferase 1 using [3H]myristoyl-CoA and GCGGSKVKPQPPQAK(biotin)-amide as substrate preincubated for 5 mins prior substrate addition measured after 50 mins by streptavidin-coated scintillation proximity assay
Measurement: IC50 > 100000 nM (pChEMBL 4)
Descriptors: MW 461.37, ALogP 5.36, HBA 5, HBD 1, PSA 76.88, QED 0.44