Synonym
PF-750; PF 750; PF750
IUPAC/Chemical Name
1-Piperidinecarboxamide, N-phenyl-4-(3-quinolinylmethyl)-
InChi Key
BIODYGOZWZNCAG-UHFFFAOYSA-N
InChi Code
InChI=1S/C22H23N3O/c26-22(24-20-7-2-1-3-8-20)25-12-10-17(11-13-25)14-18-15-19-6-4-5-9-21(19)23-16-18/h1-9,15-17H,10-14H2,(H,24,26)
SMILES Code
O=C(N1CCC(CC2=CC3=CC=CC=C3N=C2)CC1)NC4=CC=CC=C4
Purity
>98% (or refer to the Certificate of Analysis)
Shipping Condition
Shipped under ambient temperature as non-hazardous chemical. This product is stable enough for a few weeks during ordinary shipping and time spent in Customs.
Storage Condition
Dry, dark and at 0 - 4 C for short term (days to weeks) or -20 C for long term (months to years).
Solubility
Soluble in DMSO
Shelf Life
>2 years if stored properly
Drug Formulation
This drug may be formulated in DMSO
Stock Solution Storage
0 - 4 C for short term (days to weeks), or -20 C for long term (months).
HS Tariff Code
2934.99.9001
Biological target:
PF 750 is a selective and covalent fatty acid amide hydrolase (FAAH) inhibitor, with IC50s varied from 16.2-595 nM.
In vitro activity:
Herein this study describes piperidine/piperazine ureas represented by N-phenyl-4-(quinolin-3-ylmethyl)piperidine-1-carboxamide (PF-750) and N-phenyl-4-(quinolin-2-ylmethyl)piperazine-1-carboxamide (PF-622) as a novel mechanistic class of FAAH inhibitors. PF-750 and PF-622 show higher in vitro potencies than previously established classes of FAAH inhibitors. Rather unexpectedly based on the high chemical stability of the urea functional group, PF-750 and PF-622 were found to inhibit FAAH in a time-dependent manner by covalently modifying the enzyme's active site serine nucleophile. Activity-based proteomic profiling revealed that PF-750 and PF-622 were completely selective for FAAH relative to other mammalian serine hydrolases.
Reference: Biochemistry. 2007 Nov 13;46(45):13019-30. https://pubmed.ncbi.nlm.nih.gov/17949010/
|
Solvent |
mg/mL |
mM |
comments |
| Solubility |
| DMSO:PBS (pH 7.2) (1:5) |
0.1 |
0.36 |
|
| Ethanol |
1.0 |
2.89 |
|
Note: There can be variations in solubility for the same chemical from different vendors or different batches from the same vendor. The following factors can affect the solubility of the same chemical: solvent used for crystallization, residual solvent content, polymorphism, salt versus free form, degree of hydration, solvent temperature. Please use the solubility data as a reference only. Warming and sonication will facilitate dissolving. Still have questions? Please contact our Technical Support scientists.
Preparing Stock Solutions
The following data is based on the
product
molecular weight
345.45
Batch specific molecular weights may vary
from batch to batch
due to the degree of hydration, which will
affect the solvent
volumes required to prepare stock solutions.
| Concentration / Solvent Volume / Mass |
1 mg |
5 mg |
10 mg |
| 1 mM |
1.15 mL |
5.76 mL |
11.51 mL |
| 5 mM |
0.23 mL |
1.15 mL |
2.3 mL |
| 10 mM |
0.12 mL |
0.58 mL |
1.15 mL |
| 50 mM |
0.02 mL |
0.12 mL |
0.23 mL |
Formulation protocol:
Ahn K, Johnson DS, Fitzgerald LR, Liimatta M, Arendse A, Stevenson T, Lund ET, Nugent RA, Nomanbhoy TK, Alexander JP, Cravatt BF. Novel mechanistic class of fatty acid amide hydrolase inhibitors with remarkable selectivity. Biochemistry. 2007 Nov 13;46(45):13019-30. doi: 10.1021/bi701378g. Epub 2007 Oct 19. PMID: 17949010.
In vitro protocol:
Ahn K, Johnson DS, Fitzgerald LR, Liimatta M, Arendse A, Stevenson T, Lund ET, Nugent RA, Nomanbhoy TK, Alexander JP, Cravatt BF. Novel mechanistic class of fatty acid amide hydrolase inhibitors with remarkable selectivity. Biochemistry. 2007 Nov 13;46(45):13019-30. doi: 10.1021/bi701378g. Epub 2007 Oct 19. PMID: 17949010.
1: Wu H, Kelley CJ, Pino-Figueroa A, Vu HD, Maher TJ. Macamides and their synthetic analogs: evaluation of in vitro FAAH inhibition. Bioorg Med Chem. 2013 Sep 1;21(17):5188-97. doi: 10.1016/j.bmc.2013.06.034. Epub 2013 Jun 27. PubMed PMID: 23891163.
2: Feledziak M, Muccioli GG, Lambert DM, Marchand-Brynaert J. SAR and LC/MS studies of β-lactamic inhibitors of human fatty acid amide hydrolase (hFAAH): evidence of a nonhydrolytic process. J Med Chem. 2011 Oct 13;54(19):6812-23. doi: 10.1021/jm200723m. Epub 2011 Sep 20. PubMed PMID: 21899370.
3: Mileni M, Johnson DS, Wang Z, Everdeen DS, Liimatta M, Pabst B, Bhattacharya K, Nugent RA, Kamtekar S, Cravatt BF, Ahn K, Stevens RC. Structure-guided inhibitor design for human FAAH by interspecies active site conversion. Proc Natl Acad Sci U S A. 2008 Sep 2;105(35):12820-4. doi: 10.1073/pnas.0806121105. Epub 2008 Aug 27. PubMed PMID: 18753625; PubMed Central PMCID: PMC2529035.
4: Ahn K, Johnson DS, Fitzgerald LR, Liimatta M, Arendse A, Stevenson T, Lund ET, Nugent RA, Nomanbhoy TK, Alexander JP, Cravatt BF. Novel mechanistic class of fatty acid amide hydrolase inhibitors with remarkable selectivity. Biochemistry. 2007 Nov 13;46(45):13019-30. Epub 2007 Oct 19. PubMed PMID: 17949010.
5: Kodani SD, Wan D, Wagner KM, Hwang SH, Morisseau C, Hammock BD. Design and Potency of Dual Soluble Epoxide Hydrolase/Fatty Acid Amide Hydrolase Inhibitors. ACS Omega. 2018 Oct 31;3(10):14076-14086. doi: 10.1021/acsomega.8b01625. Epub 2018 Oct 25. PMID: 30411058; PMCID: PMC6210075.
