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CAS No. : | 882847-32-7 | MDL No. : | MFCD06656473 |
Formula : | C28H37NO9 | Boiling Point : | - |
Linear Structure Formula : | - | InChI Key : | TWQTXZPTZPOEEB-UHFFFAOYSA-N |
M.W : | 531.59 | Pubchem ID : | 2756187 |
Synonyms : |
|
Chemical Name : | 1-(9H-Fluoren-9-yl)-3-oxo-2,7,10,13,16,19-hexaoxa-4-azadocosan-22-oic acid |
Num. heavy atoms : | 38 |
Num. arom. heavy atoms : | 12 |
Fraction Csp3 : | 0.5 |
Num. rotatable bonds : | 22 |
Num. H-bond acceptors : | 9.0 |
Num. H-bond donors : | 2.0 |
Molar Refractivity : | 138.67 |
TPSA : | 121.78 Ų |
GI absorption : | High |
BBB permeant : | No |
P-gp substrate : | Yes |
CYP1A2 inhibitor : | No |
CYP2C19 inhibitor : | No |
CYP2C9 inhibitor : | No |
CYP2D6 inhibitor : | No |
CYP3A4 inhibitor : | Yes |
Log Kp (skin permeation) : | -8.25 cm/s |
Log Po/w (iLOGP) : | 4.79 |
Log Po/w (XLOGP3) : | 1.82 |
Log Po/w (WLOGP) : | 3.08 |
Log Po/w (MLOGP) : | 0.51 |
Log Po/w (SILICOS-IT) : | 4.57 |
Consensus Log Po/w : | 2.95 |
Lipinski : | 1.0 |
Ghose : | None |
Veber : | 1.0 |
Egan : | 0.0 |
Muegge : | 1.0 |
Bioavailability Score : | 0.56 |
Log S (ESOL) : | -3.06 |
Solubility : | 0.459 mg/ml ; 0.000863 mol/l |
Class : | Soluble |
Log S (Ali) : | -4.0 |
Solubility : | 0.0535 mg/ml ; 0.000101 mol/l |
Class : | Soluble |
Log S (SILICOS-IT) : | -7.82 |
Solubility : | 0.00000805 mg/ml ; 0.0000000151 mol/l |
Class : | Poorly soluble |
PAINS : | 0.0 alert |
Brenk : | 0.0 alert |
Leadlikeness : | 2.0 |
Synthetic accessibility : | 4.93 |
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 |
---|---|---|
General procedure: The Rink amide resin (1 equiv) was added to the reaction container, washed with DCM and DMF, and deprotected twice with 20% piperidine in DMF for 10 min each time. The Fmoc-Lys(Fmoc)-OH (5 equiv), HOBt (5 equiv) and DIC (5 equiv) were added together with 2 mL DMF and reacted for 4 h, The two Fmoc groups of lysine were deprotected and coupled with different linker (10 equiv) together with HOBt (10 equiv) and DIC (10 equiv) in 2 mL DMF for 6 h. Fmoc-NH-(PEG)mCH2CH2-COOH (MW = 443.50) was used to synthesized peptides 4-18. Different lengths of the DV3 sequence, from the C-terminal to the N-terminal, were then coupled onto the PEG linker through Fmoc-D-aa by the same method used for coupling of the linker. For peptides 15, 16, 17, and 18, the amino acid of DV3 at position 7, 8, 9, and 10 was mutated into alanine, respectively. The Fmoc groups of last amino acids acid was deprotected, and the peptide was then cleaved from the resin with the cocktail cleavage solution (TFA/H2O/Thiophenol = 90:5:5). The crude peptid ewas precipitated and washed twice with cold ethyl ether. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: The Rink amide resin (1 equiv) was added to the reaction container, washed with DCM and DMF, and deprotected twice with 20% piperidine in DMF for 10 min each time. The Fmoc-Lys(Fmoc)-OH (5 equiv), HOBt (5 equiv) and DIC (5 equiv) were added together with 2 mL DMF and reacted for 4 h, The two Fmoc groups of lysine were deprotected and coupled with different linker (10 equiv) together with HOBt (10 equiv) and DIC (10 equiv) in 2 mL DMF for 6 h. Fmoc-NH-(PEG)mCH2CH2-COOH (MW = 443.50) was used to synthesized peptides 4-18. Different lengths of the DV3 sequence, from the C-terminal to the N-terminal, were then coupled onto the PEG linker through Fmoc-D-aa by the same method used for coupling of the linker. For peptides 15, 16, 17, and 18, the amino acid of DV3 at position 7, 8, 9, and 10 was mutated into alanine, respectively. The Fmoc groups of last amino acids acid was deprotected, and the peptide was then cleaved from the resin with the cocktail cleavage solution (TFA/H2O/Thiophenol = 90:5:5). The crude peptid ewas precipitated and washed twice with cold ethyl ether. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: The Rink amide resin (1 equiv) was washed with DCM and DMF in the reaction container, and deprotected twice with 20% piperidine in DMF for 10 min each time. The Fmoc-Lys(dde)-OH (5 equiv), HOBt (5 equiv) and DIC (5 equiv) were coupled with resinin 2 mL DMF for 4 h. For peptides 21-24, one PEG linker was coupled to the N-alpha position of the first lysine using Fmoc-NH-(PEG)3-CH2CH2-COOH (MW = 443.50). The DV3 sequence from the Cterminalto the N-terminal was coupled onto the PEG linker with the last D-amino acid protected by Boc group. After the coupling of the DV3 sequence was complete, the dde group of the first coupled lysine was deprotected with 2% hydrazine in DMF. Then, the other PEG linker was coupled onto the epsilon-amino group of the first coupled lysine and the sequence of CXCL121-8 from the C-terminal to N-terminal was coupled onto the PEG linker through Fmoc-L-aa (5 equiv), HOBt (5 equiv) and DIC (5 equiv) in 2 mL DMF. For peptide 20, the DV3 and CXCL121-8 sequences was directly coupled to the alpha and epsilon amino groups of the first lysine, respectively. The Fmoc groups of last amino acids acid was deprotected before washing with DMF and DCM, then the peptide was cleaved from the resin with a cocktail cleavage solution (TFA/H2O/Thiophenol = 90:5:5) for 2 h. The crude peptide was precipitated and washed twice with cold ethyl ether. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: The Rink amide resin (1 equiv) was washed with DCM and DMF in the reaction container, and deprotected twice with 20% piperidine in DMF for 10 min each time. The Fmoc-Lys(dde)-OH (5 equiv), HOBt (5 equiv) and DIC (5 equiv) were coupled with resinin 2 mL DMF for 4 h. For peptides 21-24, one PEG linker was coupled to the N-alpha position of the first lysine using Fmoc-NH-(PEG)3-CH2CH2-COOH (MW = 443.50). The DV3 sequence from the Cterminalto the N-terminal was coupled onto the PEG linker with the last D-amino acid protected by Boc group. After the coupling of the DV3 sequence was complete, the dde group of the first coupled lysine was deprotected with 2% hydrazine in DMF. Then, the other PEG linker was coupled onto the epsilon-amino group of the first coupled lysine and the sequence of CXCL121-8 from the C-terminal to N-terminal was coupled onto the PEG linker through Fmoc-L-aa (5 equiv), HOBt (5 equiv) and DIC (5 equiv) in 2 mL DMF. For peptide 20, the DV3 and CXCL121-8 sequences was directly coupled to the alpha and epsilon amino groups of the first lysine, respectively. The Fmoc groups of last amino acids acid was deprotected before washing with DMF and DCM, then the peptide was cleaved from the resin with a cocktail cleavage solution (TFA/H2O/Thiophenol = 90:5:5) for 2 h. The crude peptide was precipitated and washed twice with cold ethyl ether. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
Fmoc-Lys--N-Dde 500 mg of resin (0.15 mmoles) was treated with 20% piperidine and then washed with DMF (3x), DCM (3x). The resin was then treated with Myristic acid (10 eq.) along with DIEA, HATU and the coupling continued for 2 hours. Dde was removed using 2% Hydrazine in DMF (2X) and then washed with DMF and DCM. Acid-PegS-Fmoc acid was then coupled using DIEA, HATU overnight. After confirming the coupling reaction withnihydrin test, Fmoc was cleaved and then the free amine is allowed to react with bromo acetic anhydride in the presence of base to generate the desired compounds FA-182 on resin. After washing with DCM (3x), the product was cleaved from the resin using 5 mL of 50% TFA in DCM containing 10% H20 and 10% triisopropylsilane for 2 h. After cleavage, the cleaved solution was died and then re-dissolved by methanol/DMF before subjecting to HPLC purification. The fractions sonjtaing the product were combined and freese dried to afford FA182 (ESI-MS calculated MW 768.2.; found 769.4 [M+1] |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
90% | With O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate; N-ethyl-N,N-diisopropylamine; In N,N-dimethyl-formamide; at 20℃; for 14h;Inert atmosphere; | Preparation of Compound 32a DIPEA (0.6 mL, 7.07 mmol) and HBTU (972 mg, 5.30 mmol) were added to a stirring mixture of compound 24g (483 mg, 0.855 mmol) and Fmoc-NH-PEG5- CH2CH2COOH (1.0 g, 3.89 mmol) in DMF (10 mL). After stirring at room temperature for 14 hours under N2, the reaction mixture was poured into H2O (30 mL) and extracted with EtOAc (3 x 30 mL). The combined organic layers were washed with 1 N aq. HCl (10 mL), saturated aq. NaHCO3 (10 mL) and brine (10 mL) sequentially, and dried over anhydrous Na2SO4. After filtration and concentration, the resulting residue was purified by column chromatography, which produced the compound 32a (1.16 g, 90 %). 1H-NMR (400 MHz, CDC13) delta 7.77 (d, 4H), 7.60(d, 4H), 7.39 (t, 4H), 7.31 (t, 4H), 4.39 (d, 4H), 4.33 (m, 1H), 4.22 (m, 2H), 4.09 (m, 2H), 3.71-3.39 (m, 52H), 3.19 (m, 2H), 2.51 (m, 4H), 1.50 (m, 1H), 1.46 (m, 1H), 1.43 (s, 9H), 1.25 (m, 2H). EI-MS m/z: [M+H]+ 1520.0. |
90% | With O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate; N-ethyl-N,N-diisopropylamine; In N,N-dimethyl-formamide; at 20℃; for 14h;Inert atmosphere; | DIPEA (0.6 mL, 7.07 mmol) and HBTU (972 mg, 5.30 mmol) were added to a stirring mixture of compound 24g (483 mg, 0.855 mmol) and Fmoc- H-PEG5- CH2CH2COOH (1.0 g, 3.89 mmol) in DMF (10 mL). After stirring at room temperature for 14 hours under N2, the reaction mixture was poured into H20 (30 mL) and extracted with EtOAc (3 x 30 mL). The combined organic layers were washed with 1 N aq. HCl (10 mL), saturated aq. NaHC03 (10 mL) and brine (10 mL) sequentially, and dried over anhydrous Na2S04. After filtration and concentration, the resulting residue was purified by column chromatography, which produced the compound 32a (1.16 g, 90 %). 1H- MR (400 MHz, CDC13) delta 7.77 (d, 4H), 7.60(d, 4H), 7.39 (t, 4H), 7.31 (t, 4H), 4.39 (d, 4H), 4.33 (m, 1H), 4.22 (m, 2H), 4.09 (m, 2H), 3.71-3.39 (m, 52H), 3.19 (m, 2H), 2.51 (m, 4H), 1.50 (m, 1H), 1.46 (m, 1H), 1.43 (s, 9H), 1.25 (m, 2H). EI-MS m/z: [M+H]+ 1520.0. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
413 mg | In a peptide synthesis vessel was added the resin, amino acid solution, iPr2NEt, and PyBOP. Argon was bubbled through the solution for 1 h and then washed 3X with DMF and IPA. A solution of 20% piperdine in DMF for FMOC deprotection was added, 2X (10mm), before each amino acid coupling. This was continued to complete all seven coupling steps.Cleavage step:25 mL of cleavage reagent (92.5% TFA, 2.5% H20, 2.5% Triisopropylsaline, 2.5% (1.34m1) ethandithiol) was added to the peptide synthesis vessel and Argon was bubbled for 1.5 h, drain, and wash 3X with cleavage reagent reagent. The reaction mixture was concentrated under reduced pressure until lOml remained. The product was triturated in ethyl ether andcentrifuge. The resulting pellet was dried under high vacuum.Deprotection step:Crude protected Compound 99 was added to lOml water. The pH adjusted to 9.3 and maintained for 1 h using potassium carbonate. After 1 h the solution was adjusted to pH 5 with iN HC1. The reaction mixture was load directly onto a C18 reverse phase column and purifiedvia with 0- 35% CH3CN/50 mM NH4HCO3 buffer, pH 7.0 to yield 413 mg Compound 99 asfluffy yellow solid. |
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