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CAS No. : | 20086-06-0 | MDL No. : | MFCD16660673 |
Formula : | C19H20O6 | Boiling Point : | - |
Linear Structure Formula : | - | InChI Key : | - |
M.W : | 344.36 | Pubchem ID : | - |
Synonyms : |
|
Chemical Name : | (2R,3aS,6S,6aS,7R,10R,11aR,11bS)-2-(Furan-3-yl)-11b-methyloctahydro-4H-3a,6:7,10-dimethanofuro[2,3-c]oxepino[4,5-e]oxepine-4,8(6H)-dione |
Num. heavy atoms : | 25 |
Num. arom. heavy atoms : | 5 |
Fraction Csp3 : | 0.68 |
Num. rotatable bonds : | 1 |
Num. H-bond acceptors : | 6.0 |
Num. H-bond donors : | 0.0 |
Molar Refractivity : | 83.83 |
TPSA : | 74.97 Ų |
GI absorption : | High |
BBB permeant : | Yes |
P-gp substrate : | No |
CYP1A2 inhibitor : | No |
CYP2C19 inhibitor : | No |
CYP2C9 inhibitor : | No |
CYP2D6 inhibitor : | Yes |
CYP3A4 inhibitor : | No |
Log Kp (skin permeation) : | -7.04 cm/s |
Log Po/w (iLOGP) : | 2.04 |
Log Po/w (XLOGP3) : | 1.91 |
Log Po/w (WLOGP) : | 2.06 |
Log Po/w (MLOGP) : | 1.62 |
Log Po/w (SILICOS-IT) : | 2.3 |
Consensus Log Po/w : | 1.98 |
Lipinski : | 0.0 |
Ghose : | None |
Veber : | 0.0 |
Egan : | 0.0 |
Muegge : | 0.0 |
Bioavailability Score : | 0.55 |
Log S (ESOL) : | -3.26 |
Solubility : | 0.189 mg/ml ; 0.000549 mol/l |
Class : | Soluble |
Log S (Ali) : | -3.11 |
Solubility : | 0.269 mg/ml ; 0.000781 mol/l |
Class : | Soluble |
Log S (SILICOS-IT) : | -3.43 |
Solubility : | 0.129 mg/ml ; 0.000374 mol/l |
Class : | Soluble |
PAINS : | 0.0 alert |
Brenk : | 1.0 alert |
Leadlikeness : | 0.0 |
Synthetic accessibility : | 5.92 |
Signal Word: | Warning | Class: | N/A |
Precautionary Statements: | P261-P305+P351+P338 | UN#: | N/A |
Hazard Statements: | H302-H315-H319-H335 | Packing Group: | N/A |
GHS Pictogram: |
* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With glucose-6-phosphate dehydrogenase; alpha-D-glucose 6-phosphate; human liver CYP3A4 enzyme, recombinant; NADPH; magnesium chloride; In aq. buffer; at 37.0℃; for 1.0h;pH 7.4;Enzymatic reaction;Kinetics; | Incubations used to derive kinetic constants by the formation of M31had the following DB and P450/HLM concentrations: DB, 5, 10, 20, 40,60, 80, 100, 120, 160, 200, and 300 mM; CYP3A4, 10 pmol; CYP3A5,15 pmol; CYP2C9, 25 pmol; CYP2C19, 15 pmol; and pooled HLM, 0.2 mg/ml.Incubation solutions (100 ml), which were conducted in triplicate, weretransferred to an ice bath for 5 minutes after 1 hour at 37C, followed bythe sequential addition of 10 ml of acetonitrile containing jatrorrhizinehydrochloride (IS), 10 ml of DMSO, and 480 ml of acetonitrile. Thefollowing processing steps were similar to those of the microsomal incubations,except that the residual was reconstituted with 90 ml ofaqueous solution containing 10% DMSO and 10% acetonitrile. Thesamples were analyzed by UPLC-MS/MS (see UPLC-MS/MS Analysisfor MGCD (M31) Formation (Analysis B)). The enzyme kinetic investigationswere performed within the range of linearity with respect toconcentrations of P450 enzymes and DB, which were determined inpreliminary experiments. Parent compound conversions were within 5%at all DB concentrations. Apparent Km and Vmax were estimated by nonlinearregression using GraphPad Prism 5.0 (GraphPad Software Inc., San Diego, CA). The data were fitted to the one-enzyme Michaelis-Mentenequation:V Vmax S=Km S;or the Michaelis-Menten model with uncompetitive substrate inhibition(Venkatakrishnan et al., 2001):V Vmax SKm S S2Ks:Eadie-Hofstee transformations were used when multiple enzymes were involvedor Hill equation was more suitable. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With glucose-6-phosphate dehydrogenase; alpha-D-glucose 6-phosphate; NADPH; magnesium chloride; In acetonitrile; at 37.0℃; for 1.0h;pH 7.4;Enzymatic reaction; | proteins(1 mg/ml), and a NADPH-regenerating system that included NADPH(1 mM), glucose 6-phosphate (10 mM), and glucose-6-phosphate dehydrogenase(1 unit/ml) in buffer A (50 mM Tris-HCl, pH 7.4, containing 4 mM MgCl2) orbuffer B (100 mM phosphate buffer, pH 7.4, containing 4 mM MgCl2). DB wasdissolved in acetonitrile, and the final concentration of acetonitrile in the incubationsystem was ,1%. The system was preincubated for 5 minutes at 37Cand initiated by adding NADPH. Control incubations were conducted withoutDB or NADPH. Incubations were stopped after 1 hour by the addition of 500 ml of ice-cold acetonitrile and then vortex-mixed for 1 minute. Denatured proteinswere separated by centrifugation at 16,000g for 10 minutes. The supernatant(540 ml) was evaporated to dryness under a nitrogen stream, reconstitutedusing 90 ml of 10% acetonitrile, vortex-mixed for 1 minute, and centrifugedat 16,000g at 4C for 10 minutes. The supernatant (5 ml) was injected into theUPLC-MS/MS system for analysis (see UPLC-MS/MS Analysis to ScreenMetabolites In Vitro and In Vivo (Analysis A)). Trapping experiments were conducted in the presence of nucleophiles,including GSH and methoxylamine (each at 10 mM), and the samples wereprepared by the aforementioned procedure. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With glucose-6-phosphate dehydrogenase; alpha-D-glucose 6-phosphate; NADPH; magnesium chloride; In acetonitrile; at 37.0℃; for 1.0h;pH 7.4;Enzymatic reaction; | proteins(1 mg/ml), and a NADPH-regenerating system that included NADPH(1 mM), glucose 6-phosphate (10 mM), and glucose-6-phosphate dehydrogenase(1 unit/ml) in buffer A (50 mM Tris-HCl, pH 7.4, containing 4 mM MgCl2) orbuffer B (100 mM phosphate buffer, pH 7.4, containing 4 mM MgCl2). DB wasdissolved in acetonitrile, and the final concentration of acetonitrile in the incubationsystem was ,1%. The system was preincubated for 5 minutes at 37Cand initiated by adding NADPH. Control incubations were conducted withoutDB or NADPH. Incubations were stopped after 1 hour by the addition of 500 ml of ice-cold acetonitrile and then vortex-mixed for 1 minute. Denatured proteinswere separated by centrifugation at 16,000g for 10 minutes. The supernatant(540 ml) was evaporated to dryness under a nitrogen stream, reconstitutedusing 90 ml of 10% acetonitrile, vortex-mixed for 1 minute, and centrifugedat 16,000g at 4C for 10 minutes. The supernatant (5 ml) was injected into theUPLC-MS/MS system for analysis (see UPLC-MS/MS Analysis to ScreenMetabolites In Vitro and In Vivo (Analysis A)). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With glucose-6-phosphate dehydrogenase; alpha-D-glucose 6-phosphate; NADPH; magnesium chloride; In acetonitrile; at 37.0℃; for 1.0h;pH 7.4;Enzymatic reaction; | proteins(1 mg/ml), and a NADPH-regenerating system that included NADPH(1 mM), glucose 6-phosphate (10 mM), and glucose-6-phosphate dehydrogenase(1 unit/ml) in buffer A (50 mM Tris-HCl, pH 7.4, containing 4 mM MgCl2) orbuffer B (100 mM phosphate buffer, pH 7.4, containing 4 mM MgCl2). DB wasdissolved in acetonitrile, and the final concentration of acetonitrile in the incubationsystem was ,1%. The system was preincubated for 5 minutes at 37Cand initiated by adding NADPH. Control incubations were conducted withoutDB or NADPH. Incubations were stopped after 1 hour by the addition of 500 ml of ice-cold acetonitrile and then vortex-mixed for 1 minute. Denatured proteinswere separated by centrifugation at 16,000g for 10 minutes. The supernatant(540 ml) was evaporated to dryness under a nitrogen stream, reconstitutedusing 90 ml of 10% acetonitrile, vortex-mixed for 1 minute, and centrifugedat 16,000g at 4C for 10 minutes. The supernatant (5 ml) was injected into theUPLC-MS/MS system for analysis (see UPLC-MS/MS Analysis to ScreenMetabolites In Vitro and In Vivo (Analysis A)). Trapping experiments were conducted in the presence of nucleophiles,including GSH and methoxylamine (each at 10 mM), and the samples wereprepared by the aforementioned procedure. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With 3,3-dimethyldioxirane; In acetone; at 20.0℃; for 2.0h;Cooling with ice; | DB (10 mg, 0.029 mmol) was dissolved in2 ml of acetone and precooled in a dry ice bath for 1 minute. Then 1.2 mlof DMDO was added immediately. The reaction mixture was allowed towarm up to room temperature and left to stand for 2 hours. A 200-mlaliquot of the reaction mixture was evaporated to dryness under nitrogenstream and reconstituted using 200 ml of 10% acetonitrile for UPLC-MS/MSanalysis (see UPLC-MS/MS Analysis to Screen Metabolites In Vitro and In Vivo(Analysis A)) to confirm the disappearance of DB. The residual DMDO wasbubbled off in the stream of nitrogen gas. The total volume was reduced to0.5 ml and used immediately for the next step. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With glucose-6-phosphate dehydrogenase; alpha-D-glucose 6-phosphate; NADPH; magnesium chloride; In aq. phosphate buffer; acetonitrile; at 37.0℃; for 1.0h;pH 7.4;Enzymatic reaction; | proteins(1 mg/ml), and a NADPH-regenerating system that included NADPH(1 mM), glucose 6-phosphate (10 mM), and glucose-6-phosphate dehydrogenase(1 unit/ml) in buffer A (50 mM Tris-HCl, pH 7.4, containing 4 mM MgCl2) orbuffer B (100 mM phosphate buffer, pH 7.4, containing 4 mM MgCl2). DB wasdissolved in acetonitrile, and the final concentration of acetonitrile in the incubationsystem was ,1%. The system was preincubated for 5 minutes at 37Cand initiated by adding NADPH. Control incubations were conducted withoutDB or NADPH. Incubations were stopped after 1 hour by the addition of 500 ml of ice-cold acetonitrile and then vortex-mixed for 1 minute. Denatured proteinswere separated by centrifugation at 16,000g for 10 minutes. The supernatant(540 ml) was evaporated to dryness under a nitrogen stream, reconstitutedusing 90 ml of 10% acetonitrile, vortex-mixed for 1 minute, and centrifugedat 16,000g at 4C for 10 minutes. The supernatant (5 ml) was injected into theUPLC-MS/MS system for analysis (see UPLC-MS/MS Analysis to ScreenMetabolites In Vitro and In Vivo (Analysis A)). |
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