Detailed information for compound 1716700
Basic information
Technical information
- Name: Unnamed compound
- MW: 364.474 | Formula: C20H25FO3S
-
H donors: 0
H acceptors: 2
LogP: 5.9
Rotable bonds: 11
Rule of 5 violations (Lipinski): 1 - SMILES: FS(=O)(=O)CCCCCCCc1cccc(c1)OCc1ccccc1
- InChi: 1S/C20H25FO3S/c21-25(22,23)15-8-3-1-2-5-10-18-13-9-14-20(16-18)24-17-19-11-6-4-7-12-19/h4,6-7,9,11-14,16H,1-3,5,8,10,15,17H2
- InChiKey: CEOCDYLHZFETSF-UHFFFAOYSA-N
Network
Hover on a compound node to display the structore
Synonyms
No synonyms found for this compound
Targets
Known targets for this compound
| Species | Target name | Source | Bibliographic reference |
|---|---|---|---|
| Rattus norvegicus | Cannabinoid CB1 receptor | Starlite/ChEMBL | References |
| Mus musculus | cannabinoid receptor 2 (macrophage) | Starlite/ChEMBL | References |
| Homo sapiens | monoglyceride lipase | Starlite/ChEMBL | References |
| Rattus norvegicus | Anandamide amidohydrolase | Starlite/ChEMBL | No references |
Predicted pathogen targets for this compound
By orthology
By sequence similarity to non orthologous known druggable targets
| Species | Potential target | Known druggable target | Length | Alignment span | Identity |
|---|---|---|---|---|---|
| Plasmodium falciparum | esterase, putative | monoglyceride lipase | 303 aa | 254 aa | 19.7 % |
| Echinococcus multilocularis | fatty acid amide hydrolase 1 | Anandamide amidohydrolase | 579 aa | 470 aa | 28.3 % |
| Onchocerca volvulus | Anandamide amidohydrolase | 579 aa | 539 aa | 34.7 % | |
| Schistosoma japonicum | Fatty-acid amide hydrolase 1, putative | Anandamide amidohydrolase | 579 aa | 499 aa | 24.6 % |
| Echinococcus granulosus | fatty acid amide hydrolase 1 | Anandamide amidohydrolase | 579 aa | 470 aa | 28.7 % |
Obtained from network model
Ranking Plot
Putative Targets List
| Species | Potential target | Raw | Global | Species |
|---|---|---|---|---|
| Plasmodium falciparum | esterase, putative | 0.0084 | 0.641 | 1 |
| Echinococcus granulosus | fatty acid amide hydrolase 1 | 0.0123 | 1 | 1 |
| Trichomonas vaginalis | Clan SC, family S33, methylesterase-like serine peptidase | 0.0084 | 0.641 | 0.5 |
| Loa Loa (eye worm) | hypothetical protein | 0.0123 | 1 | 1 |
| Mycobacterium ulcerans | lysophospholipase | 0.0084 | 0.641 | 1 |
| Wolbachia endosymbiont of Brugia malayi | aspartyl/glutamyl-tRNA amidotransferase subunit A | 0.0015 | 0 | 0.5 |
| Plasmodium vivax | PST-A protein | 0.0084 | 0.641 | 1 |
| Trichomonas vaginalis | conserved hypothetical protein | 0.0084 | 0.641 | 0.5 |
| Trypanosoma cruzi | monoglyceride lipase, putative | 0.0084 | 0.641 | 1 |
| Plasmodium falciparum | lysophospholipase, putative | 0.0084 | 0.641 | 1 |
| Trichomonas vaginalis | Clan SC, family S33, methylesterase-like serine peptidase | 0.0084 | 0.641 | 0.5 |
| Chlamydia trachomatis | glutamyl-tRNA(Gln) amidotransferase subunit A | 0.0015 | 0 | 0.5 |
| Mycobacterium tuberculosis | Possible lysophospholipase | 0.0084 | 0.641 | 1 |
| Plasmodium falciparum | lysophospholipase, putative | 0.0084 | 0.641 | 1 |
| Echinococcus multilocularis | fatty acid amide hydrolase 1 | 0.0123 | 1 | 1 |
| Entamoeba histolytica | hydrolase, alpha/beta fold family domain containing protein | 0.0084 | 0.641 | 0.5 |
| Echinococcus multilocularis | fatty acid amide hydrolase 1 | 0.0123 | 1 | 1 |
| Mycobacterium ulcerans | hypothetical protein | 0.0084 | 0.641 | 1 |
| Trichomonas vaginalis | conserved hypothetical protein | 0.0084 | 0.641 | 0.5 |
| Trichomonas vaginalis | Clan SC, family S33, methylesterase-like serine peptidase | 0.0084 | 0.641 | 0.5 |
| Mycobacterium leprae | POSSIBLE LYSOPHOSPHOLIPASE | 0.0084 | 0.641 | 1 |
| Trichomonas vaginalis | Clan SC, family S33, methylesterase-like serine peptidase | 0.0084 | 0.641 | 0.5 |
| Treponema pallidum | aspartyl/glutamyl-tRNA amidotransferase subunit A | 0.0015 | 0 | 0.5 |
| Plasmodium falciparum | lysophospholipase, putative | 0.0084 | 0.641 | 1 |
| Echinococcus granulosus | fatty acid amide hydrolase 1 | 0.0123 | 1 | 1 |
| Schistosoma mansoni | amidase | 0.0123 | 1 | 1 |
| Trypanosoma brucei | monoglyceride lipase, putative | 0.0084 | 0.641 | 1 |
| Schistosoma mansoni | fatty-acid amide hydrolase | 0.0123 | 1 | 1 |
| Trichomonas vaginalis | Clan SC, family S33, methylesterase-like serine peptidase | 0.0084 | 0.641 | 0.5 |
| Trichomonas vaginalis | valacyclovir hydrolase, putative | 0.0084 | 0.641 | 0.5 |
| Leishmania major | monoglyceride lipase, putative | 0.0084 | 0.641 | 1 |
| Trypanosoma brucei | monoglyceride lipase, putative | 0.0084 | 0.641 | 1 |
| Entamoeba histolytica | hydrolase, alpha/beta fold family domain containing protein | 0.0084 | 0.641 | 0.5 |
Activities
| Activity type | Activity value | Assay description | Source | Reference |
|---|---|---|---|---|
| IC50 (binding) | = 165 nM | BindingDB_Patents: Enzyme Assay. All compound solutions are made to a concentration of 10 mM in DMSO. To test the stability of the compounds in enzyme assay conditions, 25 nmoles of the compound are incubated in TME buffer with 0.1% BSA (final volume of 250 uL) for 15 minutes at 37 C. Samples (100 uL) are taken at the start of the assay and after 15 minutes, diluted 1:5 with acetonitrile and centrifuged (20,000 RCF, five minutes, room temperature) to precipitate the proteins. The resulting supernatant is injected onto the HPLC. Calculations for determining the percent compound remaining are described in the following equation:% R=Peak Area (T15)/Peak Area (T0)To determine whether or not the compounds are good substrates for FAAH, 25 nmoles of the compound were incubated with 75 ug enzyme preparation in TME buffer with 0.1% BSA (final volume 250 uL). The reaction mixture is treated in the same manner as described above. | ChEMBL. | No reference |
| IC50 (binding) | = 165 nM | BindingDB_Patents: Enzyme Assay. All compound solutions are made to a concentration of 10 mM in DMSO. To test the stability of the compounds in enzyme assay conditions, 25 nmoles of the compound are incubated in TME buffer with 0.1% BSA (final volume of 250 uL) for 15 minutes at 37 C. Samples (100 uL) are taken at the start of the assay and after 15 minutes, diluted 1:5 with acetonitrile and centrifuged (20,000 RCF, five minutes, room temperature) to precipitate the proteins. The resulting supernatant is injected onto the HPLC. Calculations for determining the percent compound remaining are described in the following equation:% R=Peak Area (T15)/Peak Area (T0)To determine whether or not the compounds are good substrates for FAAH, 25 nmoles of the compound were incubated with 75 ug enzyme preparation in TME buffer with 0.1% BSA (final volume 250 uL). The reaction mixture is treated in the same manner as described above. | ChEMBL. | No reference |
| IC50 (binding) | = 165 nM | BindingDB_Patents: Enzyme Assay. All compound solutions are made to a concentration of 10 mM in DMSO. To test the stability of the compounds in enzyme assay conditions, 25 nmoles of the compound are incubated in TME buffer with 0.1% BSA (final volume of 250 uL) for 15 minutes at 37 C. Samples (100 uL) are taken at the start of the assay and after 15 minutes, diluted 1:5 with acetonitrile and centrifuged (20,000 RCF, five minutes, room temperature) to precipitate the proteins. The resulting supernatant is injected onto the HPLC. Calculations for determining the percent compound remaining are described in the following equation:% R=Peak Area (T15)/Peak Area (T0)To determine whether or not the compounds are good substrates for FAAH, 25 nmoles of the compound were incubated with 75 ug enzyme preparation in TME buffer with 0.1% BSA (final volume 250 uL). The reaction mixture is treated in the same manner as described above. | ChEMBL. | No reference |
| IC50 (binding) | = 193 nM | BindingDB_Patents: Enzyme Assay. All compound solutions are made to a concentration of 10 mM in DMSO. To test the stability of the compounds in enzyme assay conditions, 25 nmoles of the compound are incubated in TME buffer with 0.1% BSA (final volume of 250 uL) for 15 minutes at 37 C. Samples (100 uL) are taken at the start of the assay and after 15 minutes, diluted 1:5 with acetonitrile and centrifuged (20,000 RCF, five minutes, room temperature) to precipitate the proteins. The resulting supernatant is injected onto the HPLC. Calculations for determining the percent compound remaining are described in the following equation:% R=Peak Area (T15)/Peak Area (T0)To determine whether or not the compounds are good substrates for FAAH, 25 nmoles of the compound were incubated with 75 ug enzyme preparation in TME buffer with 0.1% BSA (final volume 250 uL). The reaction mixture is treated in the same manner as described above. | ChEMBL. | No reference |
| IC50 (binding) | = 193 nM | BindingDB_Patents: Enzyme Assay. All compound solutions are made to a concentration of 10 mM in DMSO. To test the stability of the compounds in enzyme assay conditions, 25 nmoles of the compound are incubated in TME buffer with 0.1% BSA (final volume of 250 uL) for 15 minutes at 37 C. Samples (100 uL) are taken at the start of the assay and after 15 minutes, diluted 1:5 with acetonitrile and centrifuged (20,000 RCF, five minutes, room temperature) to precipitate the proteins. The resulting supernatant is injected onto the HPLC. Calculations for determining the percent compound remaining are described in the following equation:% R=Peak Area (T15)/Peak Area (T0)To determine whether or not the compounds are good substrates for FAAH, 25 nmoles of the compound were incubated with 75 ug enzyme preparation in TME buffer with 0.1% BSA (final volume 250 uL). The reaction mixture is treated in the same manner as described above. | ChEMBL. | No reference |
| IC50 (binding) | = 752.1 nM | Inhibition of recombinant human hexahistidine-tagged MGL expressed in Escherichia coli using AHMMCE as substrate after 15 mins by medium throughput fluorescent assay | ChEMBL. | 23083016 |
| Ki (binding) | = 39 nM | BindingDB_Patents: Enzyme Assay. All compound solutions are made to a concentration of 10 mM in DMSO. To test the stability of the compounds in enzyme assay conditions, 25 nmoles of the compound are incubated in TME buffer with 0.1% BSA (final volume of 250 uL) for 15 minutes at 37 C. Samples (100 uL) are taken at the start of the assay and after 15 minutes, diluted 1:5 with acetonitrile and centrifuged (20,000 RCF, five minutes, room temperature) to precipitate the proteins. The resulting supernatant is injected onto the HPLC. Calculations for determining the percent compound remaining are described in the following equation:% R=Peak Area (T15)/Peak Area (T0)To determine whether or not the compounds are good substrates for FAAH, 25 nmoles of the compound were incubated with 75 ug enzyme preparation in TME buffer with 0.1% BSA (final volume 250 uL). The reaction mixture is treated in the same manner as described above. | ChEMBL. | No reference |
| Ki (binding) | = 39 nM | BindingDB_Patents: Enzyme Assay. All compound solutions are made to a concentration of 10 mM in DMSO. To test the stability of the compounds in enzyme assay conditions, 25 nmoles of the compound are incubated in TME buffer with 0.1% BSA (final volume of 250 uL) for 15 minutes at 37 C. Samples (100 uL) are taken at the start of the assay and after 15 minutes, diluted 1:5 with acetonitrile and centrifuged (20,000 RCF, five minutes, room temperature) to precipitate the proteins. The resulting supernatant is injected onto the HPLC. Calculations for determining the percent compound remaining are described in the following equation:% R=Peak Area (T15)/Peak Area (T0)To determine whether or not the compounds are good substrates for FAAH, 25 nmoles of the compound were incubated with 75 ug enzyme preparation in TME buffer with 0.1% BSA (final volume 250 uL). The reaction mixture is treated in the same manner as described above. | ChEMBL. | No reference |
| Ki (binding) | = 39 nM | BindingDB_Patents: Enzyme Assay. All compound solutions are made to a concentration of 10 mM in DMSO. To test the stability of the compounds in enzyme assay conditions, 25 nmoles of the compound are incubated in TME buffer with 0.1% BSA (final volume of 250 uL) for 15 minutes at 37 C. Samples (100 uL) are taken at the start of the assay and after 15 minutes, diluted 1:5 with acetonitrile and centrifuged (20,000 RCF, five minutes, room temperature) to precipitate the proteins. The resulting supernatant is injected onto the HPLC. Calculations for determining the percent compound remaining are described in the following equation:% R=Peak Area (T15)/Peak Area (T0)To determine whether or not the compounds are good substrates for FAAH, 25 nmoles of the compound were incubated with 75 ug enzyme preparation in TME buffer with 0.1% BSA (final volume 250 uL). The reaction mixture is treated in the same manner as described above. | ChEMBL. | No reference |
| Ki (binding) | = 46 nM | BindingDB_Patents: Enzyme Assay. All compound solutions are made to a concentration of 10 mM in DMSO. To test the stability of the compounds in enzyme assay conditions, 25 nmoles of the compound are incubated in TME buffer with 0.1% BSA (final volume of 250 uL) for 15 minutes at 37 C. Samples (100 uL) are taken at the start of the assay and after 15 minutes, diluted 1:5 with acetonitrile and centrifuged (20,000 RCF, five minutes, room temperature) to precipitate the proteins. The resulting supernatant is injected onto the HPLC. Calculations for determining the percent compound remaining are described in the following equation:% R=Peak Area (T15)/Peak Area (T0)To determine whether or not the compounds are good substrates for FAAH, 25 nmoles of the compound were incubated with 75 ug enzyme preparation in TME buffer with 0.1% BSA (final volume 250 uL). The reaction mixture is treated in the same manner as described above. | ChEMBL. | No reference |
| Ki (binding) | = 46 nM | BindingDB_Patents: Enzyme Assay. All compound solutions are made to a concentration of 10 mM in DMSO. To test the stability of the compounds in enzyme assay conditions, 25 nmoles of the compound are incubated in TME buffer with 0.1% BSA (final volume of 250 uL) for 15 minutes at 37 C. Samples (100 uL) are taken at the start of the assay and after 15 minutes, diluted 1:5 with acetonitrile and centrifuged (20,000 RCF, five minutes, room temperature) to precipitate the proteins. The resulting supernatant is injected onto the HPLC. Calculations for determining the percent compound remaining are described in the following equation:% R=Peak Area (T15)/Peak Area (T0)To determine whether or not the compounds are good substrates for FAAH, 25 nmoles of the compound were incubated with 75 ug enzyme preparation in TME buffer with 0.1% BSA (final volume 250 uL). The reaction mixture is treated in the same manner as described above. | ChEMBL. | No reference |
| Ki (binding) | = 99 nM | Displacement of [3H]CP-55,940 from mouse CB2 receptor expressed in HEK293 cells | ChEMBL. | 23083016 |
| Ki (binding) | = 335 nM | Displacement of [3H]CP-55,940 from CB1 receptor in rat brain homogenates | ChEMBL. | 23083016 |
Phenotypes
Whole-cell/tissue/organism interactions
We have no records of whole-cell/tissue assays done with this compound
What does this mean?
Many chemical entities in TDR Targets come from high-throughput screenings with whole cells or tissue samples, and not all assayed compounds have been tested against a single a single target protein, probably because they get ruled out during screening process. Even if these compounds may have not been of interest in the original screening, they may come as interesting leads for other screening assays. Furthermore, we may be able to propose drug-target associations using chemical similarities and network patterns.
Annotated phenotypes:
We have no manually annotated phenotypes for this drug.
What does this mean? / Care to help?
In TDR Targets, information about phenotypes that are caused by
drugs, or by genetic manipulation of cells (e.g. gene knockouts or
knockdowns) is manually curated from the literature. These
descriptions help to describe the potential of the target for drug
development. If no information is available for this gene or if the
information is incomplete, this may mean that i) the papers
containing this information either appeared after the curation
effort for this organism was carried out or they were inadvertently
missed by curators; or that ii) the curation effort for this
organism has not yet started.
In any case, if you have information about papers containing relevant validation data for this target, please log in using your TDR Targets username and password and send them to us using the corresponding form in this page (only visible to registered users) or contact us.
In any case, if you have information about papers containing relevant validation data for this target, please log in using your TDR Targets username and password and send them to us using the corresponding form in this page (only visible to registered users) or contact us.
External resources for this compound
- ChEMBL: CHEMBL2180831
Bibliographic References
1 literature reference was collected for this gene.
If you have references for this compound, please enter them in a user comment (below) or Contact us.