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[ CAS No. 171859-74-8 ] {[proInfo.proName]}

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Cat. No.: {[proInfo.prAm]}
Chemical Structure| 171859-74-8
Chemical Structure| 171859-74-8
Structure of 171859-74-8 * Storage: {[proInfo.prStorage]}
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Product Details of [ 171859-74-8 ]

CAS No. :171859-74-8 MDL No. :MFCD03548229
Formula : C25H21NO4 Boiling Point : -
Linear Structure Formula :- InChI Key :-
M.W : 399.44 Pubchem ID :-
Synonyms :

Safety of [ 171859-74-8 ]

Signal Word:Warning Class:
Precautionary Statements:P261-P264-P271-P280-P302+P352-P304+P340-P305+P351+P338-P312-P332+P313-P337+P313-P362-P403+P233-P405-P501 UN#:
Hazard Statements:H315-H319-H335 Packing Group:
GHS Pictogram:

Application In Synthesis of [ 171859-74-8 ]

* 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.

  • Downstream synthetic route of [ 171859-74-8 ]

[ 171859-74-8 ] Synthesis Path-Downstream   1~7

  • 1
  • [ 99953-00-1 ]
  • [ 71989-14-5 ]
  • [ 76-05-1 ]
  • [ 171859-74-8 ]
  • (R)-3-({2-[(S)-2-Amino-3-(4-hydroxy-2,6-dimethyl-phenyl)-propionyl]-1,2,3,4-tetrahydro-isoquinoline-3-carbonyl}-amino)-succinamic acid; compound with trifluoro-acetic acid [ No CAS ]
  • 2
  • [ 99953-00-1 ]
  • [ 104091-08-9 ]
  • [ 76-05-1 ]
  • [ 171859-74-8 ]
  • (R)-4-({2-[(S)-2-Amino-3-(4-hydroxy-2,6-dimethyl-phenyl)-propionyl]-1,2,3,4-tetrahydro-isoquinoline-3-carbonyl}-amino)-4-carbamoyl-butyric acid; compound with trifluoro-acetic acid [ No CAS ]
  • 3
  • C11H15N2O3PolS [ No CAS ]
  • [ 84000-07-7 ]
  • [ 132684-60-7 ]
  • [ 171859-74-8 ]
  • C31H42N5O6PolS [ No CAS ]
YieldReaction ConditionsOperation in experiment
General procedure: Peptides were synthesized on a CEM Liberty automated microwave peptide synthesizer (CEM Microwave Technology Ltd, Buckingham, England, UK). In essence, each peptide was synthesised, on a 0.1-0.5mmol scale, using either Rink Amide MBHA resin (substitution 0.65 mmol/g, 100-200mesh) for peptides (18-20) or a pre-loaded 4-Sulfamylbutyryl AM resin (substitution 0.6-0.8 mmol/g, loaded as described under Section 2.1.2) for peptides (10a) and (11a-f). Fmoc removal was performed using 2 repeat cycles employing 20% (V/V) piperidine as solution in DMF. A first deprotection cycle of 30 s at 50W was employed, followed by a second deprotection cycle of 3min at 50W. Both cycles were carried out at 75C. Coupling steps were carried out by introducing each Fmoc-amino acid (0.2M solution in DMF) at a fivefold excess over resin loading, together with HBTU activation reagent and DIEA activation base used in the molar ratios HBTU/DIEA/AA (1/2/1). Each coupling reaction was performed for 10min, at 22W, at 75C. Finally, cleavage of peptides (18-20) from Rink Amide MBHA was performed manually, at room temperature, using TFA/H2O/triisopropylsilane (95/2.5/2.5, v/v/v), for two 1h cycles, with washing with dichloromethane after every cycle. The collected cleavage reaction mixtures and washes were evaporated under vacuum, at 30C, cooled, and the products precipitated by the addition of cold diethylether. The precipitates were collected by centrifugation (3-5 min at 2000-3000 g) and the pellet washed thoroughly with diethylether. This process was repeated 2-3 times, each time the solid was collected by centrifugation. On the other hand, cleavage of peptides 10a and 11a-f from 4-Sulfamylbutyryl AM resin was performed as described under Section 2.1.3. After a brief drying in vacuum to remove all traces of solvents, the peptide products were dissolved in 10% TFA aqueous solution and freeze dried. Peptide purity was checked through RP-HPLC, using Waters HPLC system fitted with Waters 1525 binary HPLC pump and Waters 2489 UV/visible detector (lambda216 nm) (Waters, Milford, Massachusetts, USA) and employing a Phenomenex Jupiter C12 column (250 ×4.66mm; particle size, 10mum). The runs were carried out on an analytical scale with a flow rate of 1ml/min. An elution gradient was utilized to resolve the crude product components that went from 90% solvent A (0.05% TFA in H2O)/10% Solvent B (0.05% TFA in CH3OH) to 10% solvent A/90% solvent B in 60min. Peptides with crude purity less than 95% were purified with semi-preparative RP-HPLC, using Phenomenex Jupiter C12 column (250 ×21.20mm; particle size, 10mum) and using the same above stated elution gradient with a flow rate of 10ml/min. 2.1.2 General procedure for 4-sulfamylbutyryl AM ?Safety-Catch? resin loading. 4-Sulfamylbutyryl AM Resin (625mg, 0.5mmol) suspended in 17ml CHCl3, DIEA (476.6mul, 2.5mmol) and an Fmoc-amino acid [(2S,4R)-Fmoc-4-phenyl-pyrrolidine-2-carboxylic acid (620mg, 1.5mmol); (2S,4S)-Fmoc-4-phenoxy-pyrrolidine-2-carboxylic acid (643mg, 1.5mmol); Fmoc-Tic-OH (600mg, 1.5mmol)] were added to a 100ml round bottom flask. The reaction mixture was stirred for 10min, cooled to -20C and after 20min PyBop (780mg, 1.5mmol) was added as solid. The reaction mixture was stirred for 8h at -20C after which the resin was filtered and washed with CHCl3 (3 ×5ml). The resin was dried in a desiccator under vacuum. The resin loading was checked spectrophotometrically by performing Fmoc-group removal on accurately weighed samples (?4mg) of resin derivatized by these three Fmoc-derivatives, and measuring the formation of the dibenzofulvene-piperidine adduct (molar absorptivity epsilon=5253M-1cm-1 at lambda290nm), using a UV spectrophotometer (50 Scan UV-Visible Spectrophotometer, VARIAN, Australia).
  • 4
  • H-Gly-(2-Cl)-Trt-pol [ No CAS ]
  • [ 86060-81-3 ]
  • [ 171859-74-8 ]
  • C18H24N4O5S [ No CAS ]
  • 5
  • [ 77128-70-2 ]
  • [ 171859-74-8 ]
  • C16H21N3O4S [ No CAS ]
YieldReaction ConditionsOperation in experiment
93% Stage #1: N-(9-fluorenylmethoxycarbonyl)sarcosine With N-ethyl-N,N-diisopropylamine In dichloromethane; N,N-dimethyl-formamide at 20℃; for 1h; Stage #2: With piperidine In N,N-dimethyl-formamide Stage #3: N-Fmoc-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid; Fmoc-Cys(pg)-OH Further stages;
  • 6
  • [ 94744-50-0 ]
  • [ 171859-74-8 ]
  • Fmoc-Cys(pg)-OH [ No CAS ]
  • C17H23N3O4S [ No CAS ]
  • 7
  • Fmoc-β-Ala-Wang resin [ No CAS ]
  • [ 108-24-7 ]
  • [ 118358-38-6 ]
  • fmoc-azetidine-3-carboxylic acid [ No CAS ]
  • [ 171859-74-8 ]
  • Fmoc-Arg(*)-OH [ No CAS ]
  • Ac-RAzRRAzRRZS*RAzRAzRB, Az= 3-azetidinecarboxylic acid, Z= 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid, S*= L-serine glycosylated with D-glucose [ No CAS ]
YieldReaction ConditionsOperation in experiment
Peptides were synthesized on a 100 μηιοΙ scale using a CEM Liberty microwave Peptide Synthesizer (Buckingham, UK) and Fmoc chemistry following manufacturer's recommendations. The side chain protecting groups used were labile to trifluoroacetic acid treatment and the peptide was synthesized using a 5-fold excess of Fmoc-protected amino acids (0.25 mmol) that were activated using PyBOP (5-fold excess) in the presence of DIPEA or with DIC|Oxyma. Piperidine (20% v/v in DMF) was used to remove N-Fmoc protecting groups. The coupling was carried out once at 75 C for 5 min at 60-watt microwave power except for arginine and the glycosylated amino acid residues, which were coupled twice each. (0452) Histidine and cysteine residues were coupled once at 50C for 5 min at 60-watt microwave power. Each deprotection reaction was carried out at 75 C twice, once for 30 sec and then for 3 min at 35-watt microwave power. Once synthesis was complete, the resin was washed with DMF (3 x 50 mL) and the N-terminus of the solid phase bound peptide was acetylated with acetic anhydride in the presence of DIPEA. The peptide was cleaved from the solid support by treatment with a cleavage cocktail consisting of trifluoroacetic acid (TFA): 3,6- dioxa-1 ,8-octanedithiol (DODT): H20: triisopropylsilane (TIPS) (94%: 2.5%: 2.5%: 1 %, 10 mL) or trifluoroacetic acid (TFA): H20: m-cresol: triisopropylsilane (TIPS) (94%: 2.5%: 2.5%: 1 %, (0453) 1 mL) or trifluoroacetic acid (TFA): H20: triisopropylsilane (TIPS) (96.5%: 2.5%: 1 %, 1 mL) for (0454) 2 h at room temperature for 2-3 h at room temperature. Excess TFA was removed by blowing N2 through the peptide solution. The cleaved peptide was precipitated via the addition of ice- cold diethyl ether and centrifuged at 3000 rpm for 5 min. The peptide pellet was washed in ice-cold diethyl ether thrice. The crude peptide was dissolved in water, analyzed and purified by RP-HPLC on Phenomenex Jupiter column (21.2 X 250 mm, C18, 10 μηι) at a flow rate of 20 mL/min with the following gradient (A: 0.1 % TFA, B: 90% CH3CN, 0.1 % TFA) 0-2 min 5% B 2-35 min 5%-60% B 35-40 min 60%-90% B used. The fractions containing the desired peptide were combined and lyophilized to give the product as a white solid.
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