lovingscience/chembl-v37-raw-activities huggingface dataset:
Compound (SMILES): C[C@H](NC(=O)c1c(=O)oc(O)c2cccc(-c3cccc(C(F)(F)F)c3)c12)C(=O)O
InChIKey: LSWVVTOUEOQJRU-VIFPVBQESA-N
Target: Protease (SINGLE PROTEIN), Human immunodeficiency virus 1
UniProt: Q9YQ12
Assay: Enzymatic Assay : This is a fluorometric assay based on the cleavage by protease of a substrate carrying a donor group (EDANS) and an acceptor group (DABCYL) on each side of the cleavage site, interacting together through fluorescence resonance energy transfer (FRET) as described by Matayoshi et al. (Science 247:954-954, 1990).
Measurement: IC50 = 1.353 nM (pChEMBL 8.869999885559082)
Descriptors: MW 421.33, ALogP 3.39, HBA 5, HBD 3, PSA 116.84, QED 0.59
Compound (SMILES): Cc1ccccc1C[C@H](NC(=O)c1cccc(C)c1O)C(=O)NCCCC[C@@H](CO)N(CC(C)C)S(=O)(=O)c1ccc(N)cc1
InChIKey: GIXNFUDXKSHSST-IZEXYCQBSA-N
Target: Protease (SINGLE PROTEIN), Human immunodeficiency virus 1
UniProt: Q9YQ12
Assay: Enzymatic Assay : This is a fluorometric assay based on the cleavage by protease of a substrate carrying a donor group (EDANS) and an acceptor group (DABCYL) on each side of the cleavage site, interacting together through fluorescence resonance energy transfer (FRET) as described by Matayoshi et al. (Science 247:954-954, 1990).
Measurement: IC50 = 4.122 nM (pChEMBL 8.380000114440918)
Descriptors: MW 638.83, ALogP 3.93, HBA 7, HBD 5, PSA 162.06, QED 0.12
Compound (SMILES): Cc1ccc(C(=O)N[C@@H](Cc2ccccc2C)C(=O)NCCCC[C@@H](CO)N(CC(C)C)S(=O)(=O)c2ccc(N)cc2)cc1O
InChIKey: BQTNMTPSQXOGPM-SMCANUKXSA-N
Target: Protease (SINGLE PROTEIN), Human immunodeficiency virus 1
UniProt: Q9YQ12
Assay: Enzymatic Assay : This is a fluorometric assay based on the cleavage by protease of a substrate carrying a donor group (EDANS) and an acceptor group (DABCYL) on each side of the cleavage site, interacting together through fluorescence resonance energy transfer (FRET) as described by Matayoshi et al. (Science 247:954-954, 1990).
Measurement: IC50 = 0.938 nM (pChEMBL 9.029999732971191)
Descriptors: MW 638.83, ALogP 3.93, HBA 7, HBD 5, PSA 162.06, QED 0.12
Compound (SMILES): COC(=O)N[C@@H](CC1CCCCC1)C(=O)NCCCC[C@@H](CO)N(CC(C)C)S(=O)(=O)c1ccc(N)cc1
InChIKey: MUGPCJSECROUMS-ZCYQVOJMSA-N
Target: Protease (SINGLE PROTEIN), Human immunodeficiency virus 1
UniProt: Q9YQ12
Assay: Enzymatic Assay : This is a fluorometric assay based on the cleavage by protease of a substrate carrying a donor group (EDANS) and an acceptor group (DABCYL) on each side of the cleavage site, interacting together through fluorescence resonance energy transfer (FRET) as described by Matayoshi et al. (Science 247:954-954, 1990).
Measurement: IC50 = 5.212 nM (pChEMBL 8.279999732971191)
Descriptors: MW 554.75, ALogP 3.26, HBA 7, HBD 4, PSA 151.06, QED 0.19
Compound (SMILES): CC(C)CN([C@H](CO)CCCCNC(=O)[C@H](CC1CCCCC1)NC(=O)c1cccnc1)S(=O)(=O)c1ccc(N)cc1
InChIKey: NIQQXGQUHFDUNP-YTMVLYRLSA-N
Target: Protease (SINGLE PROTEIN), Human immunodeficiency virus 1
UniProt: Q9YQ12
Assay: Enzymatic Assay : This is a fluorometric assay based on the cleavage by protease of a substrate carrying a donor group (EDANS) and an acceptor group (DABCYL) on each side of the cleavage site, interacting together through fluorescence resonance energy transfer (FRET) as described by Matayoshi et al. (Science 247:954-954, 1990).
Measurement: IC50 = 2.876 nM (pChEMBL 8.539999961853027)
Descriptors: MW 601.81, ALogP 3.73, HBA 7, HBD 4, PSA 154.72, QED 0.17
Compound (SMILES): Cc1ccc(C(=O)N[C@@H](CC2CCCCC2)C(=O)NCCCC[C@@H](CO)N(CC(C)C)S(=O)(=O)c2ccc(N)cc2)cn1
InChIKey: JJSAKJLNMPHIKK-JDXGNMNLSA-N
Target: Protease (SINGLE PROTEIN), Human immunodeficiency virus 1
UniProt: Q9YQ12
Assay: Enzymatic Assay : This is a fluorometric assay based on the cleavage by protease of a substrate carrying a donor group (EDANS) and an acceptor group (DABCYL) on each side of the cleavage site, interacting together through fluorescence resonance energy transfer (FRET) as described by Matayoshi et al. (Science 247:954-954, 1990).
Measurement: IC50 = 3.314 nM (pChEMBL 8.479999542236328)
Descriptors: MW 615.84, ALogP 4.04, HBA 7, HBD 4, PSA 154.72, QED 0.16
Compound (SMILES): C[C@]1(c2cc(NC3CCc4cc(Cl)cnc43)ccc2F)N=C(N)COC[C@@H]1F
InChIKey: LLVAUXCCVYNQFH-KKOVZHJLSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 70 nM (pChEMBL 7.159999847412109)
Descriptors: MW 406.86, ALogP 3.91, HBA 5, HBD 2, PSA 72.53, QED 0.81
Compound (SMILES): C[C@]1(c2cc(NCc3nn(C(F)F)cc3Cl)ccc2F)N=C(N)COC[C@@H]1F
InChIKey: RZXYOIJGPYTNGY-WMLDXEAASA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 40 nM (pChEMBL 7.400000095367432)
Descriptors: MW 419.81, ALogP 3.62, HBA 6, HBD 2, PSA 77.46, QED 0.73
Compound (SMILES): C[C@]1(c2cc(NC3CCOC3)ccc2F)N=C(N)COC[C@@H]1F
InChIKey: UPNYTQSKKDHJPL-TWZNPMNKSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 72 nM (pChEMBL 7.139999866485596)
Descriptors: MW 325.36, ALogP 1.97, HBA 5, HBD 2, PSA 68.87, QED 0.89
Compound (SMILES): C[C@]1(c2cc(NC3CCCOC3)ccc2F)N=C(N)COC[C@@H]1F
InChIKey: JPKWXEFYYHRRRJ-BRCNOLGNSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 73 nM (pChEMBL 7.139999866485596)
Descriptors: MW 339.39, ALogP 2.36, HBA 5, HBD 2, PSA 68.87, QED 0.89
Compound (SMILES): C[C@]1(c2cc(NC3CCOCC3)ccc2F)N=C(N)COC[C@@H]1F
InChIKey: AOUYERQDQWXFRI-DOTOQJQBSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 2400 nM (pChEMBL 5.619999885559082)
Descriptors: MW 339.39, ALogP 2.36, HBA 5, HBD 2, PSA 68.87, QED 0.89
Compound (SMILES): C[C@]1(c2cc(NCc3nn(C(F)F)cc3Cl)ccc2F)N=C(N)COCC1(F)F
InChIKey: JQFSKBFJRFOZRE-MRXNPFEDSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 11 nM (pChEMBL 7.960000038146973)
Descriptors: MW 437.8, ALogP 3.92, HBA 6, HBD 2, PSA 77.46, QED 0.7
Compound (SMILES): CC[C@]1(c2cc(NCc3nn(C(F)F)cc3Cl)ccc2F)N=C(N)COCC1(F)F
InChIKey: NUVPFLZJJVXOTE-QGZVFWFLSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 170 nM (pChEMBL 6.769999980926514)
Descriptors: MW 451.83, ALogP 4.31, HBA 6, HBD 2, PSA 77.46, QED 0.64
Compound (SMILES): C[C@]1(c2cc(N[C@H]3CCc4cc(Cl)cnc43)ccc2F)N=C(N)COCC1(F)F
InChIKey: MRMHPBKPLSGSSO-QFBILLFUSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 30 nM (pChEMBL 7.519999980926514)
Descriptors: MW 424.85, ALogP 4.21, HBA 5, HBD 2, PSA 72.53, QED 0.77
Compound (SMILES): C[C@]1(c2cc(N[C@@H]3CCc4cc(Cl)cnc43)ccc2F)N=C(N)COCC1(F)F
InChIKey: MRMHPBKPLSGSSO-VQIMIIECSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 650 nM (pChEMBL 6.190000057220459)
Descriptors: MW 424.85, ALogP 4.21, HBA 5, HBD 2, PSA 72.53, QED 0.77
Compound (SMILES): C[C@]1(c2cc(Nc3ccc(C#N)cc3)ccc2F)N=C(N)COCC1(F)F
InChIKey: LBGFFZGJEKCFTP-GOSISDBHSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 910 nM (pChEMBL 6.039999961853027)
Descriptors: MW 374.37, ALogP 3.68, HBA 5, HBD 2, PSA 83.43, QED 0.86
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(N[C@H]3CCc4cc(C#N)cnc43)ccc2F)C1(F)F
InChIKey: JAWQNPDVHXPUOL-PGRDOPGGSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 5 nM (pChEMBL 8.300000190734863)
Descriptors: MW 443.47, ALogP 4.21, HBA 6, HBD 2, PSA 96.32, QED 0.74
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(N[C@@H]3CCc4cc(C#N)cnc43)ccc2F)C1(F)F
InChIKey: JAWQNPDVHXPUOL-XMSQKQJNSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 2810 nM (pChEMBL 5.550000190734863)
Descriptors: MW 443.47, ALogP 4.21, HBA 6, HBD 2, PSA 96.32, QED 0.74
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(NC3CCc4cc(Cl)cnc43)ccc2F)C1(F)F
InChIKey: QEQRMWYXLWHPTH-FBLFFUNLSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 28 nM (pChEMBL 7.550000190734863)
Descriptors: MW 452.91, ALogP 4.99, HBA 5, HBD 2, PSA 72.53, QED 0.69
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(NC3COc4cc(Cl)cnc43)ccc2F)C1(F)F
InChIKey: KGAFYWZDTGMPJU-YQYDADCPSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 58 nM (pChEMBL 7.239999771118164)
Descriptors: MW 454.88, ALogP 4.44, HBA 6, HBD 2, PSA 81.76, QED 0.72
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(NC3CCCc4cc(C#N)cnc43)ccc2F)C1(F)F
InChIKey: DQDFNCUEKCQXCI-LEQGEALCSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 133 nM (pChEMBL 6.880000114440918)
Descriptors: MW 457.5, ALogP 4.6, HBA 6, HBD 2, PSA 96.32, QED 0.7
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(NC3COc4cc(Cl)ccc43)ccc2F)C1(F)F
InChIKey: ONHMGVGQADMHCB-FBLFFUNLSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 320 nM (pChEMBL 6.5)
Descriptors: MW 453.89, ALogP 5.04, HBA 5, HBD 2, PSA 68.87, QED 0.68
Compound (SMILES): Cn1ccc(Nc2ccc(F)c([C@@]3(C)N=C(N)COC(C)(C)C3(F)F)c2)n1
InChIKey: QYGFFWAZNLLMIB-QGZVFWFLSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 530 nM (pChEMBL 6.28000020980835)
Descriptors: MW 381.4, ALogP 3.32, HBA 6, HBD 2, PSA 77.46, QED 0.86
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(Nc3ccc(F)cc3)ccc2F)C1(F)F
InChIKey: CFNQAYSORUWKLN-LJQANCHMSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 310 nM (pChEMBL 6.510000228881836)
Descriptors: MW 395.4, ALogP 4.72, HBA 4, HBD 2, PSA 59.64, QED 0.74
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(N[C@H]3CCc4cc(C#N)cnc43)c(F)cc2F)C1(F)F
InChIKey: ZXPMSLQQIPEYLP-HTAPYJJXSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 1900 nM (pChEMBL 5.71999979019165)
Descriptors: MW 461.46, ALogP 4.35, HBA 6, HBD 2, PSA 96.32, QED 0.66
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(Nc3ccc(Cl)nc3)ccc2F)C1(F)F
InChIKey: ZHRCZUUYWIYZLZ-GOSISDBHSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 370 nM (pChEMBL 6.429999828338623)
Descriptors: MW 412.84, ALogP 4.63, HBA 5, HBD 2, PSA 72.53, QED 0.72
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(Nc3cncc(F)c3)ccc2F)C1(F)F
InChIKey: QDHCAUCHZFEKAE-GOSISDBHSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 440 nM (pChEMBL 6.360000133514404)
Descriptors: MW 396.39, ALogP 4.12, HBA 5, HBD 2, PSA 72.53, QED 0.77
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(Nc3cccnc3)ccc2F)C1(F)F
InChIKey: XOQWCIWXRUAODU-GOSISDBHSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 940 nM (pChEMBL 6.03000020980835)
Descriptors: MW 378.4, ALogP 3.98, HBA 5, HBD 2, PSA 72.53, QED 0.85
Compound (SMILES): COc1ccc(Nc2ccc(F)c([C@@]3(C)N=C(N)COC(C)(C)C3(F)F)c2)cn1
InChIKey: POSSNERCWDVBPP-LJQANCHMSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 1630 nM (pChEMBL 5.789999961853027)
Descriptors: MW 408.42, ALogP 3.99, HBA 6, HBD 2, PSA 81.76, QED 0.8
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(Nc3cncc(C(F)(F)F)c3)ccc2F)C1(F)F
InChIKey: GDPOMHIELXXKQZ-GOSISDBHSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 1900 nM (pChEMBL 5.71999979019165)
Descriptors: MW 446.4, ALogP 5, HBA 5, HBD 2, PSA 72.53, QED 0.65
Compound (SMILES): Cc1ccc(Nc2ccc(F)c([C@@]3(C)N=C(N)COC(C)(C)C3(F)F)c2)cn1
InChIKey: JRBMREFVXABBQM-LJQANCHMSA-N
Target: Beta-secretase 1 (SINGLE PROTEIN), Homo sapiens
UniProt: P56817
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 5900 nM (pChEMBL 5.230000019073486)
Descriptors: MW 392.43, ALogP 4.29, HBA 5, HBD 2, PSA 72.53, QED 0.82
Compound (SMILES): CC1(C)OCC(N)=N[C@](C)(c2cc(Nc3ccc(OCC(F)(F)F)nc3)ccc2F)C1(F)F
InChIKey: WBZPQQJIWRFYNT-LJQANCHMSA-N
Target: Beta-secretase 2 (SINGLE PROTEIN), Homo sapiens
UniProt: Q9Y5Z0
Assay: Immunofluorescence Resonance Energy Transfer (FRET) Assay: The FRET assay was performed essentially as described in Gruninger-Leitch et al., Journal of Biological Chemistry (2002) 277(7) 4687-93 (Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases). In summary, a peptide is designed that is cleaved by the protease. The peptide is labelled with dabcyl at the N terminus and Lucifer Yellow at the C-terminus, such that for an intact peptide the Lucifer Yellow fluorescence is quenched by the dabcyl. When the peptide is cut by BACE2, the quenching is removed and a fluorescent signal is generated. The assay was performed as described in Grueninger et al. 2002 at pH 4.5 using a substrate concentration of 5 μM. A FRET peptide based on the TMEM27 sequence was devised. dabcyl-QTLEFLKIPS-LucY (SEQ ID NO: 1). BACE2 had a high activity against this sequence, which is unrelated to the known APP-based substrates. Conversely, BACE1 had insignificant activity against this peptide.
Measurement: IC50 = 1493 nM (pChEMBL 5.829999923706055)
Descriptors: MW 476.42, ALogP 4.92, HBA 6, HBD 2, PSA 81.76, QED 0.6
Compound (SMILES): CCc1nn2c(C)cc(C)nc2c1Cc1ccc(/C=C/C2(O)CCN(C(=O)OC(C)(C)C)CC2)cc1
InChIKey: AQGKSOBZBXOUSV-OUKQBFOZSA-N
Target: G-prodeshotein coupled receptor 4 (SINGLE PROTEIN), Homo sapiens
UniProt: P46093
Assay: Radio Ligand Binding Assay: Serial dilutions of compounds (stock in 10 mM DMSO) are prepared by first diluting the compounds in DMSO followed by a 1:50 dilution into assay buffer (10 mM HEPES, pH 8.0, 100 mM NaCl, 5 mM MgCl2, 1 mM CaCl2, 0.5% fatty acid-free BSA, 0.05% Tween-20). The radioligand [3H]4 (example 39) (specific activity 1500 GBq/mmol) is diluted directly into the assay buffer immediately before use to obtain a 20 nM solution. The desired amount of membranes (20 μg/well) is diluted with assay buffer. 50 μL of pre-diluted compound and 50 μL of [3H]4 (example 39) is placed into the bottom of a 96-well well plate. 100 μL of the membrane-suspension is added and the plate stirred for 60 minutes. The reaction is stopped by transfer onto the filter of a 96-well GF/C filter plate (soaked for 1 hour in 0.25% PEI) using a cell harvester.
Measurement: IC50 = 45 nM (pChEMBL 7.349999904632568)
Descriptors: MW 490.65, ALogP 5.27, HBA 6, HBD 1, PSA 79.96, QED 0.53
Compound (SMILES): CCc1nn2c(C)cc(C)nc2c1Cc1ccc(/C=C/CC2(O)CN(C(=O)OC(C)(C)C)C2)cc1
InChIKey: IEQJKNPISFJISW-CMDGGOBGSA-N
Target: G-prodeshotein coupled receptor 4 (SINGLE PROTEIN), Homo sapiens
UniProt: P46093
Assay: Radio Ligand Binding Assay: Serial dilutions of compounds (stock in 10 mM DMSO) are prepared by first diluting the compounds in DMSO followed by a 1:50 dilution into assay buffer (10 mM HEPES, pH 8.0, 100 mM NaCl, 5 mM MgCl2, 1 mM CaCl2, 0.5% fatty acid-free BSA, 0.05% Tween-20). The radioligand [3H]4 (example 39) (specific activity 1500 GBq/mmol) is diluted directly into the assay buffer immediately before use to obtain a 20 nM solution. The desired amount of membranes (20 μg/well) is diluted with assay buffer. 50 μL of pre-diluted compound and 50 μL of [3H]4 (example 39) is placed into the bottom of a 96-well well plate. 100 μL of the membrane-suspension is added and the plate stirred for 60 minutes. The reaction is stopped by transfer onto the filter of a 96-well GF/C filter plate (soaked for 1 hour in 0.25% PEI) using a cell harvester.
Measurement: IC50 = 34 nM (pChEMBL 7.46999979019165)
Descriptors: MW 476.62, ALogP 4.88, HBA 6, HBD 1, PSA 79.96, QED 0.55
Compound (SMILES): CCc1nn2c(C)cc(C)nc2c1Cc1ccc(/C=C/CC2(O)CCNCC2)cc1
InChIKey: CBCJTISJWHFCOC-AATRIKPKSA-N
Target: G-prodeshotein coupled receptor 4 (SINGLE PROTEIN), Homo sapiens
UniProt: P46093
Assay: Radio Ligand Binding Assay: Serial dilutions of compounds (stock in 10 mM DMSO) are prepared by first diluting the compounds in DMSO followed by a 1:50 dilution into assay buffer (10 mM HEPES, pH 8.0, 100 mM NaCl, 5 mM MgCl2, 1 mM CaCl2, 0.5% fatty acid-free BSA, 0.05% Tween-20). The radioligand [3H]4 (example 39) (specific activity 1500 GBq/mmol) is diluted directly into the assay buffer immediately before use to obtain a 20 nM solution. The desired amount of membranes (20 μg/well) is diluted with assay buffer. 50 μL of pre-diluted compound and 50 μL of [3H]4 (example 39) is placed into the bottom of a 96-well well plate. 100 μL of the membrane-suspension is added and the plate stirred for 60 minutes. The reaction is stopped by transfer onto the filter of a 96-well GF/C filter plate (soaked for 1 hour in 0.25% PEI) using a cell harvester.
Measurement: IC50 = 44 nM (pChEMBL 7.360000133514404)
Descriptors: MW 404.56, ALogP 4.02, HBA 5, HBD 2, PSA 62.45, QED 0.65
Compound (SMILES): CCc1nn2c(C)cc(C)nc2c1Cc1ccc(CCCC2(O)CCN(C(=O)OC(C)(C)C)CC2)cc1
InChIKey: JNYMFWUBRIAGIH-UHFFFAOYSA-N
Target: G-prodeshotein coupled receptor 4 (SINGLE PROTEIN), Homo sapiens
UniProt: P46093
Assay: Radio Ligand Binding Assay: Serial dilutions of compounds (stock in 10 mM DMSO) are prepared by first diluting the compounds in DMSO followed by a 1:50 dilution into assay buffer (10 mM HEPES, pH 8.0, 100 mM NaCl, 5 mM MgCl2, 1 mM CaCl2, 0.5% fatty acid-free BSA, 0.05% Tween-20). The radioligand [3H]4 (example 39) (specific activity 1500 GBq/mmol) is diluted directly into the assay buffer immediately before use to obtain a 20 nM solution. The desired amount of membranes (20 μg/well) is diluted with assay buffer. 50 μL of pre-diluted compound and 50 μL of [3H]4 (example 39) is placed into the bottom of a 96-well well plate. 100 μL of the membrane-suspension is added and the plate stirred for 60 minutes. The reaction is stopped by transfer onto the filter of a 96-well GF/C filter plate (soaked for 1 hour in 0.25% PEI) using a cell harvester.
Measurement: IC50 = 47 nM (pChEMBL 7.329999923706055)
Descriptors: MW 506.69, ALogP 5.58, HBA 6, HBD 1, PSA 79.96, QED 0.45
Compound (SMILES): CCc1nn2c(C)cc(C)nc2c1Cc1ccc(/C=C/C[C@]2(O)CCN[C@@H](C)C2)cc1
InChIKey: LXMWEIWZNWWODN-JNCWXOIASA-N
Target: G-prodeshotein coupled receptor 4 (SINGLE PROTEIN), Homo sapiens
UniProt: P46093
Assay: Radio Ligand Binding Assay: Serial dilutions of compounds (stock in 10 mM DMSO) are prepared by first diluting the compounds in DMSO followed by a 1:50 dilution into assay buffer (10 mM HEPES, pH 8.0, 100 mM NaCl, 5 mM MgCl2, 1 mM CaCl2, 0.5% fatty acid-free BSA, 0.05% Tween-20). The radioligand [3H]4 (example 39) (specific activity 1500 GBq/mmol) is diluted directly into the assay buffer immediately before use to obtain a 20 nM solution. The desired amount of membranes (20 μg/well) is diluted with assay buffer. 50 μL of pre-diluted compound and 50 μL of [3H]4 (example 39) is placed into the bottom of a 96-well well plate. 100 μL of the membrane-suspension is added and the plate stirred for 60 minutes. The reaction is stopped by transfer onto the filter of a 96-well GF/C filter plate (soaked for 1 hour in 0.25% PEI) using a cell harvester.
Measurement: IC50 = 15 nM (pChEMBL 7.820000171661377)
Descriptors: MW 418.59, ALogP 4.41, HBA 5, HBD 2, PSA 62.45, QED 0.62
Compound (SMILES): CCc1nn2c(C)cc(C)nc2c1Cc1ccc(/C=C/CC2(O)CCN(C[C@@H](O)CO)CC2)cc1
InChIKey: UNCNIMAKVCFORU-QQHIZMLBSA-N
Target: G-prodeshotein coupled receptor 4 (SINGLE PROTEIN), Homo sapiens
UniProt: P46093
Assay: Radio Ligand Binding Assay: Serial dilutions of compounds (stock in 10 mM DMSO) are prepared by first diluting the compounds in DMSO followed by a 1:50 dilution into assay buffer (10 mM HEPES, pH 8.0, 100 mM NaCl, 5 mM MgCl2, 1 mM CaCl2, 0.5% fatty acid-free BSA, 0.05% Tween-20). The radioligand [3H]4 (example 39) (specific activity 1500 GBq/mmol) is diluted directly into the assay buffer immediately before use to obtain a 20 nM solution. The desired amount of membranes (20 μg/well) is diluted with assay buffer. 50 μL of pre-diluted compound and 50 μL of [3H]4 (example 39) is placed into the bottom of a 96-well well plate. 100 μL of the membrane-suspension is added and the plate stirred for 60 minutes. The reaction is stopped by transfer onto the filter of a 96-well GF/C filter plate (soaked for 1 hour in 0.25% PEI) using a cell harvester.
Measurement: IC50 = 24 nM (pChEMBL 7.619999885559082)
Descriptors: MW 478.64, ALogP 3.08, HBA 7, HBD 3, PSA 94.12, QED 0.44
Compound (SMILES): CCc1nn2c(C)cc(C)nc2c1Cc1ccc(/C=C/CC2(O)CCN(C(=O)CN(C)C(=O)OC(C)(C)C)CC2)cc1
InChIKey: APNDVRBAKRJWQQ-MDZDMXLPSA-N
Target: G-prodeshotein coupled receptor 4 (SINGLE PROTEIN), Homo sapiens
UniProt: P46093
Assay: Radio Ligand Binding Assay: Serial dilutions of compounds (stock in 10 mM DMSO) are prepared by first diluting the compounds in DMSO followed by a 1:50 dilution into assay buffer (10 mM HEPES, pH 8.0, 100 mM NaCl, 5 mM MgCl2, 1 mM CaCl2, 0.5% fatty acid-free BSA, 0.05% Tween-20). The radioligand [3H]4 (example 39) (specific activity 1500 GBq/mmol) is diluted directly into the assay buffer immediately before use to obtain a 20 nM solution. The desired amount of membranes (20 μg/well) is diluted with assay buffer. 50 μL of pre-diluted compound and 50 μL of [3H]4 (example 39) is placed into the bottom of a 96-well well plate. 100 μL of the membrane-suspension is added and the plate stirred for 60 minutes. The reaction is stopped by transfer onto the filter of a 96-well GF/C filter plate (soaked for 1 hour in 0.25% PEI) using a cell harvester.
Measurement: IC50 = 34 nM (pChEMBL 7.46999979019165)
Descriptors: MW 575.75, ALogP 5.12, HBA 7, HBD 1, PSA 100.27, QED 0.4
Compound (SMILES): CCc1nn2c(C)cc(C)nc2c1Cc1ccc(/C=C/CN2CCN[C@H](CO)C2)cc1
InChIKey: BNRHMRYRONRUHO-BDNZGDGKSA-N
Target: G-prodeshotein coupled receptor 4 (SINGLE PROTEIN), Homo sapiens
UniProt: P46093
Assay: Radio Ligand Binding Assay: Serial dilutions of compounds (stock in 10 mM DMSO) are prepared by first diluting the compounds in DMSO followed by a 1:50 dilution into assay buffer (10 mM HEPES, pH 8.0, 100 mM NaCl, 5 mM MgCl2, 1 mM CaCl2, 0.5% fatty acid-free BSA, 0.05% Tween-20). The radioligand [3H]4 (example 39) (specific activity 1500 GBq/mmol) is diluted directly into the assay buffer immediately before use to obtain a 20 nM solution. The desired amount of membranes (20 μg/well) is diluted with assay buffer. 50 μL of pre-diluted compound and 50 μL of [3H]4 (example 39) is placed into the bottom of a 96-well well plate. 100 μL of the membrane-suspension is added and the plate stirred for 60 minutes. The reaction is stopped by transfer onto the filter of a 96-well GF/C filter plate (soaked for 1 hour in 0.25% PEI) using a cell harvester.
Measurement: IC50 = 28 nM (pChEMBL 7.550000190734863)
Descriptors: MW 419.57, ALogP 2.78, HBA 6, HBD 2, PSA 65.69, QED 0.62