* 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.
Reference：
[1] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[2] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[3] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[4] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[5] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[6] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[7] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[8] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[9] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[10] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[11] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[12] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[13] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[14] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[15] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[16] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[17] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[18] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[19] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[20] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[21] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[22] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[23] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
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[25] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[26] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
2
[ 100-02-7 ]
[ 57-11-4 ]
[ 14617-86-8 ]
Reference：
[1] Bulletin of the Academy of Sciences of the USSR, Division of Chemical Science (English Translation), 1990, vol. 39, # 11, p. 2311 - 2316[2] Izvestiya Akademii Nauk SSSR, Seriya Khimicheskaya, 1990, # 11, p. 2555 - 2560
[3] Comptes Rendus Chimie, 2013, vol. 16, # 3, p. 229 - 238
[4] Journal of Molecular Catalysis B: Enzymatic, 2011, vol. 73, # 1-4, p. 22 - 26
[5] Australian Journal of Chemistry, 1975, vol. 28, p. 1011 - 1015
[6] Journal of Organic Chemistry, 1970, vol. 35, p. 2042 - 2043
[7] Chemische Berichte, 1963, vol. 96, p. 1747 - 1750
[8] Journal of the Chemical Society, Perkin Transactions 1: Organic and Bio-Organic Chemistry (1972-1999), 1988, p. 423 - 432
3
[ 100-02-7 ]
[ 112-76-5 ]
[ 14617-86-8 ]
Reference：
[1] Tetrahedron Letters, 1983, vol. 24, # 7, p. 719 - 722
[2] Tetrahedron, 1986, vol. 42, # 9, p. 2457 - 2468
[3] Journal of Pharmaceutical Sciences, 1982, vol. 71, # 7, p. 772 - 776
[4] Acta Chemica Scandinavica (1947-1973), 1957, vol. 11, p. 913
3-(octadecanoylamino)propyl [(5-acetamido-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosyl)onic acid]-(2->3)-β-D-galactopyranosyl-(1->4)-β-D-glucopyranoside[ No CAS ]
With Pseudomonas sp. DMVR46 lipase; In aq. phosphate buffer; isopropyl alcohol; at 37℃; for 0.166667h;Enzymatic reaction;
General procedure: The pH stat method: Lipase activity was measured under controlled temperature using a pH 718 STAT Titrino Titrator (Metrohm, Switzerland). The buffer used for the activity determination comprised of 10% (m/v) Gum Arabic, 0.2% (m/v) bile salt, and 20% (m/v) CaCl2, 5% (v/v) cotton oil as substrate and 0.1M NaOH as the titrant. The insoluble triglycerides were dispersed by vigorous stirring. One unit of enzyme activity was defined as the amount of enzyme that liberates 1mumol of fatty acid/min at 37C. In order to check hydrolytic activity of lipase exclusively for different p-nitrophenyl esters lipase activity was measured with spectrophotometric method using p-nitrophenyl esters as substrate [22]. The substrate with a final concentration of 0.3mg/mL was dissolved in 1mL of isopropanol and mixed with 9mL of 50mM sodium phosphate buffer (pH 8.5) containing gum Arabic (0.1%) and Triton X-100 (0.6%). The reaction mixture was composed of 240muL of substrate solution and 10muL of appropriately diluted enzyme solution, and incubated at 37C for 10min. The p-nitrophenol (p-NP) produced in the reaction mixture was quantified spectrophotometrically at 410nm. One unit of enzyme activity was defined as the amount of enzyme that liberated 1mumol p-nitrophenol/min under standard assay conditions.
To a solution of sphingosine-1-phosphorylcholine 14 (89.8 mg, 0.14mmol) in CH2Cl2 (1 ml) was added trifluoroacetic acid (0.62 ml, 8.4 mmol) at 0 C. After the reactionmixture was stirred for 30 min at 0 C, the reaction was quenched with Et3N (2 ml), and the resultingmixture was evaporated to give the crude amine. The crude amine was dissolved in THF (0.62 ml) andsubsequently subjected to the next reaction. To a solution of the crude amine in THF were added Et3N(58.5 mul, 0.42 mmol), DMAP (18.3 mg, 0.15 mmol), and <strong>[14617-86-8]p-nitrophenyl octadecanoate</strong> (68.9 mg, 0.17mmol). After the reaction mixture was stirred for 13 h at room temperature, the solvent was removed byevaporation. Purification by silica gel column chromatography (CHCl3/MeOH/H2O = 65/25/4) affordedprotected sphingomyelin (80.5 mg) as a white solid. Then, to a solution of the protected sphingomyelin(80.5 mg) in THF (1 ml) was added TBAF (1.0 M in THF, 0.4 ml, 0.4 mmol) at 0 C. After the reactionmixture was stirred for 26 h at room temperature, MeOH was added and the solvent was evaporated. Theresultant residue was washed with acetone on Celite-Pad and dissolved with CHCl3/MeOH (1/1). After thesolvent was evaporated, purification by silica gel column chromatography (CHCl3/MeOH/H2O = 65/25/4)afforded 3-deuterated sphingomyelin 15 (55.0 mg, 75.2 mumol 54% for 3 steps) as a white solid
In a pear-shape flask, under argon atmosphere, Boc-protected amine (122 mg, 0.17 mmol) was dissolved in dry CH2Cl2 (3.4 mL) and cooled to 0 C before the addition of TFA (0.64 mL, 8.6 mmol). After 1 h at 0 C, TLC showed disappearance of starting material (Rf 0.30, 72/25/3 CHCl3/MeOH/NH4OH) and formation of a new product (Rf 0.09). The excess of TFA was removed in vacuo and then co-evaporated with benzene twice. Under argon atmosphere, the resulting brown paste was taken in dry THF (4.3 mL) and successively were added triethylamine (142 mL, 1.03 mmol), DMAP (31 mg, 0.26 mmol) and stearic activated ester (90 mg, 0.22 mmol). The mixture was stirred overnight at room temperature then precipitated in cold acetone. The white precipitate was filtered off and washed with cold acetone. Crystallisation from the crude mixture afforded sphingomyelin analogue as a white solid (80 mg, 66%).Rf: [72/25/3 CHCl3/MeOH/NH4OH]: 0.17?H (500 MHz, MeOH-d4, 303 K): 0.90 (6H, t J=6.9 Hz); 1.25-1.42 (50H, m); 1.54-1.63 (2H, m); 2.03 (2H, app q J=6.8 Hz); 2.14-2.23 (2H, m); 3.28 (6H, s); 3.55 (1H, t J=2.5 Hz); 3.74 (2H, dd J=5.3, 4.0 Hz); 3.92-3.99 (2H, m); 4.05 (1H, t J=8.2 Hz); 4.11 (1H, ddd J=10.9, 6.5, 4.8 Hz); 4.27-4.33 (2H, m); 4.44 (2H, d J=2.5 Hz); 5.45 (1H, ddt J=15.4, 7.8, 1.3 Hz); 5.71 (1H, dtd J=15.2, 6.6, 0.6 Hz); 5.96 (1H, d J=6.3 Hz).?c (125 MHz, CDCl3, 303 K): 14.4, 23.7, 27.2, 30.4-30.9, 33.1, 33.5, 37.4, 52.0, 55.3, 56.45, 60.23, 60.27, 65.34, 65.40, 65.9, 72.6, 101.3, 111.1, 131.2, 135.1, 175.9.m/z (ESI Pos): 777.7 [M+Na] 75%, 1532.0 [2M+Na] 85%.
With dmap; triethylamine; In tetrahydrofuran; at 20℃; for 24h;
SM-d9 To a solution of 7 (27 mg, 0.047 mmol) in CH2Cl2 (1.2 mL) was added trifluoroacetic acid (0.24 mL) 0C. After stirring at the same temperature for 1h, the reaction mixture was concentrated. The residue was diluted with THF (1.2 mL), and then triethylamine (40 muL, 0.28 mmol), DMAP (8.6 mg, 0.07 mmol) and <strong>[14617-86-8]p-nitrophenyl stearate</strong> (28.6 mg, 0.07 mmol) were added to the reaction mixture. After stirring at room temperature for 24 h, the residue was concentrated under reduced pressure and purified by flash column chromatography on silica gel (CH2Cl2/MeOH = 6:4 then CH2Cl2/MeOH/NH4OH = 60:40:5) to afford 3 (20 mg, 58%) as a white solid.
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