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[ CAS No. 130369-36-7 ] {[proInfo.proName]}

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Chemical Structure| 130369-36-7
Chemical Structure| 130369-36-7
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Product Details of [ 130369-36-7 ]

CAS No. :130369-36-7 MDL No. :MFCD13152267
Formula : C12H13NO3 Boiling Point : -
Linear Structure Formula :- InChI Key :PSAMWNBBHLUISE-UHFFFAOYSA-N
M.W :219.24 Pubchem ID :19794323
Synonyms :

Calculated chemistry of [ 130369-36-7 ]

Physicochemical Properties

Num. heavy atoms : 16
Num. arom. heavy atoms : 6
Fraction Csp3 : 0.33
Num. rotatable bonds : 5
Num. H-bond acceptors : 3.0
Num. H-bond donors : 1.0
Molar Refractivity : 58.0
TPSA : 55.4 Ų

Pharmacokinetics

GI absorption : High
BBB permeant : Yes
P-gp substrate : No
CYP1A2 inhibitor : No
CYP2C19 inhibitor : No
CYP2C9 inhibitor : No
CYP2D6 inhibitor : No
CYP3A4 inhibitor : No
Log Kp (skin permeation) : -6.96 cm/s

Lipophilicity

Log Po/w (iLOGP) : 1.98
Log Po/w (XLOGP3) : 0.96
Log Po/w (WLOGP) : 1.49
Log Po/w (MLOGP) : 1.06
Log Po/w (SILICOS-IT) : 1.77
Consensus Log Po/w : 1.45

Druglikeness

Lipinski : 0.0
Ghose : None
Veber : 0.0
Egan : 0.0
Muegge : 0.0
Bioavailability Score : 0.55

Water Solubility

Log S (ESOL) : -1.75
Solubility : 3.88 mg/ml ; 0.0177 mol/l
Class : Very soluble
Log S (Ali) : -1.71
Solubility : 4.27 mg/ml ; 0.0195 mol/l
Class : Very soluble
Log S (SILICOS-IT) : -3.32
Solubility : 0.106 mg/ml ; 0.000482 mol/l
Class : Soluble

Medicinal Chemistry

PAINS : 0.0 alert
Brenk : 0.0 alert
Leadlikeness : 1.0
Synthetic accessibility : 2.05

Safety of [ 130369-36-7 ]

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:

Application In Synthesis of [ 130369-36-7 ]

* 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.

  • Upstream synthesis route of [ 130369-36-7 ]
  • Downstream synthetic route of [ 130369-36-7 ]

[ 130369-36-7 ] Synthesis Path-Upstream   1~5

  • 1
  • [ 130369-36-7 ]
  • [ 87219-29-2 ]
  • [ 118399-28-3 ]
YieldReaction ConditionsOperation in experiment
32 % ee With alpha-D-glucopyranose; glucose dehydrogenase (GDH-105); Baeyere-Villiger monooxygenase P1-C06; oxygen; NADPH In methanol; aq. phosphate buffer at 30℃; for 24 h; Enzymatic reaction General procedure: Owing to the problems that both ketones 1k,l and their corresponding lactones 2k,l showed when analyzed by GC, as well as their poor solubility in diethyl ether or ethyl acetate, their enzymatic transformations were carried out in a bigger scale (3, 2 mL tubes) but maintaining identical reaction conditions. After 24 h, products were extracted with deuterated chloroform (2400 μL). The organic phases were dried over anhydrous sodium sulfate, filtered and conversion values were determined by 1H NMR experiments. Similarly, samples were evaporated and the residue re-dissolved in a mixture of hexane:ethanol 90:10 for HPLC analyses (see Tables S20-S21). In a typical experiment carried out in 1.5 mL tubes (total volume of 500 μL), the substrate 1a-j, m-v (10 mM) was dissolved in methanol (5 μL, 1percent v/v) and KPi buffer (100 mM, pH 9.0, 482 μL), containing glucose (20 mM), glucose dehydrogenase (GDH-105, 10 U, from stock solution of 1.275 U/μL), NADPH (0.2 mM, from a 20 mM stock solution) and the corresponding Baeyere-Villiger monooxygenase (2 mg). The mixture was shaken at 250 rpm at 30 °C for 24 h. The reaction was stopped by extracting with diethyl ether (2x400 μL) and centrifugedat 13,000 rpm in order to separate both phases and pellet the suspended protein. The organic phases were combined, dried over anhydrous sodium sulfate and analyzed by GC in order to determine the conversion values. Then, the solvent in GC samples was evaporated with a continuous flow of nitrogen, the residue redissolved in a mixture of hexane:ethanol 90:10 and the new sample filtered and analyzed by HPLC, leading to the measurement of the enantiomeric excess of the lactones. Control experiments in the absence of enzyme were performed for all substrates, not observing any reaction product after similar periods of time (Tables S1-S19).
78 % ee With alpha-D-glucopyranose; glucose dehydrogenase (GDH-105); Baeyere-Villiger monooxygenase P1-D08; oxygen; NADPH In methanol; aq. phosphate buffer at 30℃; for 24 h; Enzymatic reaction General procedure: Owing to the problems that both ketones 1k,l and their corresponding lactones 2k,l showed when analyzed by GC, as well as their poor solubility in diethyl ether or ethyl acetate, their enzymatic transformations were carried out in a bigger scale (3, 2 mL tubes) but maintaining identical reaction conditions. After 24 h, products were extracted with deuterated chloroform (2400 μL). The organic phases were dried over anhydrous sodium sulfate, filtered and conversion values were determined by 1H NMR experiments. Similarly, samples were evaporated and the residue re-dissolved in a mixture of hexane:ethanol 90:10 for HPLC analyses (see Tables S20-S21). In a typical experiment carried out in 1.5 mL tubes (total volume of 500 μL), the substrate 1a-j, m-v (10 mM) was dissolved in methanol (5 μL, 1percent v/v) and KPi buffer (100 mM, pH 9.0, 482 μL), containing glucose (20 mM), glucose dehydrogenase (GDH-105, 10 U, from stock solution of 1.275 U/μL), NADPH (0.2 mM, from a 20 mM stock solution) and the corresponding Baeyere-Villiger monooxygenase (2 mg). The mixture was shaken at 250 rpm at 30 °C for 24 h. The reaction was stopped by extracting with diethyl ether (2x400 μL) and centrifugedat 13,000 rpm in order to separate both phases and pellet the suspended protein. The organic phases were combined, dried over anhydrous sodium sulfate and analyzed by GC in order to determine the conversion values. Then, the solvent in GC samples was evaporated with a continuous flow of nitrogen, the residue redissolved in a mixture of hexane:ethanol 90:10 and the new sample filtered and analyzed by HPLC, leading to the measurement of the enantiomeric excess of the lactones. Control experiments in the absence of enzyme were performed for all substrates, not observing any reaction product after similar periods of time (Tables S1-S19).
Reference: [1] Tetrahedron, 2016, vol. 72, # 46, p. 7268 - 7275
[2] Tetrahedron, 2016, vol. 72, # 46, p. 7268 - 7275
  • 2
  • [ 130369-36-7 ]
  • [ 87219-29-2 ]
  • [ 118399-28-3 ]
YieldReaction ConditionsOperation in experiment
32 % ee With alpha-D-glucopyranose; glucose dehydrogenase (GDH-105); Baeyere-Villiger monooxygenase P1-C06; oxygen; NADPH In methanol; aq. phosphate buffer at 30℃; for 24 h; Enzymatic reaction General procedure: Owing to the problems that both ketones 1k,l and their corresponding lactones 2k,l showed when analyzed by GC, as well as their poor solubility in diethyl ether or ethyl acetate, their enzymatic transformations were carried out in a bigger scale (3, 2 mL tubes) but maintaining identical reaction conditions. After 24 h, products were extracted with deuterated chloroform (2400 μL). The organic phases were dried over anhydrous sodium sulfate, filtered and conversion values were determined by 1H NMR experiments. Similarly, samples were evaporated and the residue re-dissolved in a mixture of hexane:ethanol 90:10 for HPLC analyses (see Tables S20-S21). In a typical experiment carried out in 1.5 mL tubes (total volume of 500 μL), the substrate 1a-j, m-v (10 mM) was dissolved in methanol (5 μL, 1percent v/v) and KPi buffer (100 mM, pH 9.0, 482 μL), containing glucose (20 mM), glucose dehydrogenase (GDH-105, 10 U, from stock solution of 1.275 U/μL), NADPH (0.2 mM, from a 20 mM stock solution) and the corresponding Baeyere-Villiger monooxygenase (2 mg). The mixture was shaken at 250 rpm at 30 °C for 24 h. The reaction was stopped by extracting with diethyl ether (2x400 μL) and centrifugedat 13,000 rpm in order to separate both phases and pellet the suspended protein. The organic phases were combined, dried over anhydrous sodium sulfate and analyzed by GC in order to determine the conversion values. Then, the solvent in GC samples was evaporated with a continuous flow of nitrogen, the residue redissolved in a mixture of hexane:ethanol 90:10 and the new sample filtered and analyzed by HPLC, leading to the measurement of the enantiomeric excess of the lactones. Control experiments in the absence of enzyme were performed for all substrates, not observing any reaction product after similar periods of time (Tables S1-S19).
78 % ee With alpha-D-glucopyranose; glucose dehydrogenase (GDH-105); Baeyere-Villiger monooxygenase P1-D08; oxygen; NADPH In methanol; aq. phosphate buffer at 30℃; for 24 h; Enzymatic reaction General procedure: Owing to the problems that both ketones 1k,l and their corresponding lactones 2k,l showed when analyzed by GC, as well as their poor solubility in diethyl ether or ethyl acetate, their enzymatic transformations were carried out in a bigger scale (3, 2 mL tubes) but maintaining identical reaction conditions. After 24 h, products were extracted with deuterated chloroform (2400 μL). The organic phases were dried over anhydrous sodium sulfate, filtered and conversion values were determined by 1H NMR experiments. Similarly, samples were evaporated and the residue re-dissolved in a mixture of hexane:ethanol 90:10 for HPLC analyses (see Tables S20-S21). In a typical experiment carried out in 1.5 mL tubes (total volume of 500 μL), the substrate 1a-j, m-v (10 mM) was dissolved in methanol (5 μL, 1percent v/v) and KPi buffer (100 mM, pH 9.0, 482 μL), containing glucose (20 mM), glucose dehydrogenase (GDH-105, 10 U, from stock solution of 1.275 U/μL), NADPH (0.2 mM, from a 20 mM stock solution) and the corresponding Baeyere-Villiger monooxygenase (2 mg). The mixture was shaken at 250 rpm at 30 °C for 24 h. The reaction was stopped by extracting with diethyl ether (2x400 μL) and centrifugedat 13,000 rpm in order to separate both phases and pellet the suspended protein. The organic phases were combined, dried over anhydrous sodium sulfate and analyzed by GC in order to determine the conversion values. Then, the solvent in GC samples was evaporated with a continuous flow of nitrogen, the residue redissolved in a mixture of hexane:ethanol 90:10 and the new sample filtered and analyzed by HPLC, leading to the measurement of the enantiomeric excess of the lactones. Control experiments in the absence of enzyme were performed for all substrates, not observing any reaction product after similar periods of time (Tables S1-S19).
Reference: [1] Tetrahedron, 2016, vol. 72, # 46, p. 7268 - 7275
[2] Tetrahedron, 2016, vol. 72, # 46, p. 7268 - 7275
  • 3
  • [ 23761-23-1 ]
  • [ 100-51-6 ]
  • [ 130369-36-7 ]
YieldReaction ConditionsOperation in experiment
50%
Stage #1: With diphenylphosphoranyl azide; N-ethyl-N,N-diisopropylamine In toluene at 60℃; for 3 h; Inert atmosphere
Stage #2: at 60℃;
Compound 8: l-(3-((((2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4- dihydroxytetrahydrofuran-2-yl)methyl)(methyl)amino)cyclobutyl)-3-(4-(tert- butyl)phenyl)ureaBenzyl (3-oxocyclobutyl)carbamate[0665] To a solution of 3-oxocyclobutanecarboxylic acid (1.0 g, 8.77 mmol) and DIEA (1.92 g, 14.92 mmol) in toluene (8 mL) was added DPPA (2.89 g, 10.52 mmol) at rt. The mixture was heated to 60 °C under Argon for 3 h, then benzyl alcohol (1.14 g, 10.52 mmol) was added. The mixture was stirred at 60 °C overnight. The reaction was concentrated, the residue was purified by SGC (PE : EA = 8 : 1) to afford the desired compound (240 mg, yield 50percent). 1H NMR (500MHz, CDC13): δΗ 7.38-7.33 (m, 5H), 5.12 (d, / = 7.5 Hz, 2H), 4.34-4.33 (brs, 1 H), 3.44-3.39 (m, 2H), 3.10-3.07 (brs, 2H) ppm; ESI-MS (m/z): 220.2 [M+l]+.
25%
Stage #1: With diphenyl phosphoryl azide; triethylamine In toluene at 60℃; for 3 h;
Stage #2: at 60℃; for 3 h;
Step A: (3-Oxo-cyclobutyl)-carbamic acid benzyl ester. A solution of 3-Oxo- cyclobutanecarboxylic acid (1.01 g, 8.8 mmol) and Et3N (1.5ml, 10.5mmol) in THF/Toluene (1: 1, 30ml) was treated with DPPA (1.9 ml, 8.8 mmol). The mixture was stirred for 3 hours at 60°C and then BnOH (1 ml, 9.7mmol) added. The reaction mixture was stirred for another 3 hours at the same temperature. The resulting mixture was concentrated under vacuum to remove most THF and then diluted with EtOAc (50 20 ml). This so-obtained mixture was washed with saturated NaHC03 solution, brine, dried over Na2S04 and filtered. The solvent was evaporated and the residue was purified via chromatography eluted with PE/EtOAc (4: 1) to give the desired product as a white solid (yield: 0.48g, 25percent yield). 1H NMR (400 MHz, CDC13): δ 7.35 (m, 5H), 5.12 (m, 3H), 4.33 (m, 1H), 3.41 (m, 2H), 3.07 (m, 2H).
Reference: [1] Patent: WO2012/75381, 2012, A1, . Location in patent: Page/Page column 210
[2] Patent: WO2012/9678, 2012, A1, . Location in patent: Page/Page column 210
[3] Patent: EP1256578, 2002, A1, . Location in patent: Page 22
[4] Patent: WO2014/74421, 2014, A1, . Location in patent: Page/Page column 56; 57
  • 4
  • [ 96-50-4 ]
  • [ 75-77-4 ]
  • [ 130369-36-7 ]
Reference: [1] Patent: US2003/78252, 2003, A1,
  • 5
  • [ 23761-23-1 ]
  • [ 130369-36-7 ]
Reference: [1] Patent: EP1256578, 2002, A1, . Location in patent: Page 15
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