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Chemical Structure| 221884-63-5 Chemical Structure| 221884-63-5

Structure of Fmoc-DL-Gly(α-allyl)-OH
CAS No.: 221884-63-5

Chemical Structure| 221884-63-5

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Product Details of [ 221884-63-5 ]

CAS No. :221884-63-5
Formula : C20H19NO4
M.W : 337.37
SMILES Code : C=CCC(NC(OCC1C2=C(C3=C1C=CC=C3)C=CC=C2)=O)C(O)=O
MDL No. :MFCD02259489

Safety of [ 221884-63-5 ]

Application In Synthesis of [ 221884-63-5 ]

* 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 [ 221884-63-5 ]

[ 221884-63-5 ] Synthesis Path-Downstream   1~1

  • 1
  • aminomethylpolystyrene [ No CAS ]
  • [ 35661-40-6 ]
  • [ 108-24-7 ]
  • [ 71989-38-3 ]
  • [ 145069-56-3 ]
  • Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
  • [ 221884-63-5 ]
  • C82H102N11O16PolS [ No CAS ]
YieldReaction ConditionsOperation in experiment
General procedure: For the synthesis of peptides affording a C-terminal acid (1, 2, 5, 6, 9, 10, 13, 14, 17, 18, 21, 22, 25, 26), AM-PS resin was initially swollen in CH2Cl2 (30 min) and subsequently reacted with Fmoc-AA-OCH2PhOCH2CH2CO2H (2.0equiv), and DIC (2.0equiv) in CH2Cl2 (2.0mL) for 2h at room temperature.27 The Kaiser test was negative.33 For the synthesis of peptides containing C-terminal amide (3, 4, 7, 8, 11, 12, 15, 16, 19, 20, 23, 24, 27, 28, 29), AM-PS resin was initially swollen in DMF (30 min) and subsequently reacted with Rink linker (5.0 equiv), DIC (5.0 equiv), and 6-Cl-HOBt (5.0equiv) in DMF (2.0 mL) for 2h at room temperature.27 The Kaiser test was negative.33 Fmoc SPPS was then performed on a Liberty 1 Microwave Peptide Synthesiser (CEM Corporation, Mathews, NC) on a 0.1 mmol scale using the Fmoc/tBu strategy. All amino acid couplings were performed as single coupling cycles, with the exception of Fmoc-Arg(Pbf) where a double coupling cycle was performed as part of a synthetic protocol recommended by CEM Microwave Technology. All Fmoc-AA couplings were performed using Fmoc-AA (5.0equiv, 0.2M), HBTU (4.5equiv, 0.45M), and iPrNEt (10equiv, 2M) in DMF, for 5 min, at 25W and maximum temperature of 75C, except Fmoc-Arg(Pbf) that was initially coupled for 25 min at room temperature which was followed by the second coupling for 3 min, at 25W and maximum temperature of 72C. Fmoc protecting group was removed using 5% piperazine in DMF (compounds 1-4) and 5% piperazine with 0.1M 6-Cl-HOBt in DMF (compounds 5-28). A 30s deprotection cycle was followed by a second deprotection for 3 min at 62W and maximum temperature of 75C. Acetylation was performed by treatment of the resin with acetic anhydride (20% in DMF) at room temperature (2×20min), or by using acetic anhydride (0.5M in NMP), iPr2EtN (0.125M in NMP) and acatalytic quantity of HOBt in NMP (room temperature, 2×5min). A fritted glass reaction vessel was used for the manual synthesis of 29 (0.25mmol scale). The Fmoc protecting group was deprotected with 20% piperidine solution in DMF (1×5min, 1×15min). The resin was washed with DMF (5×5mL), and Fmoc-AA coupling was performed. Nalpha-Fmoc-protected amino acid (4.0 equiv) was dissolved in DMF, HCTU (3.8 equiv) was added and mixture shaken until dissolved. The solution was transferred to the reaction vessel and shaken for 2min, followed by the addition of iPr2EtN (8.0 equiv). The mixture was shaken for 45min, filtered, and washed with DMF (3×5 mL). The resulting peptides were cleaved from the resin with simultaneous side chain protecting group removal by treatment with TFA/iPr3SiH/H2O/DODT (v/v/v/v; 94/1/2.5/2.5), for 2h at room temperature. The crude peptides were precipitated and triturated with cold diethyl ether, isolated (centrifugation), dissolved in 20% acetonitrile (aq) containing 0.1% TFA and lyophilized. Analytical reverse phase high-performance liquid chromatography (RP-HPLC) was performed using either a Dionex P680 or Dionex Ultimate U3000 system (flow rate of 1mL/min), using Waters XTerra column (MS C18, 150 mm×4.6 mm; 5mum) using gradient systems as indicated in the Supporting information. The solvent system used was A (0.1% TFA in H2O) and B (0.1% TFA in acetonitrile) with detection at 210nm, 254nm, and 280nm. The ratio of products was determined by integration of spectra recorded at 210nm. A Hewlett Packard (HP) 1100MSD mass spectrometer using ESI in the positive mode spectrometer was used for ESI-MS analysis (positive mode). Peptide purification was performed using a Waters 600E system using a semipreparative Phenomenex Gemini C18, 250mm×10mm; 5mum column or Phenomenex Luna C8, 250mm×10mm; 5mum column. Gradient systems were adjusted according to the elution profiles and peak profiles obtained from the analytical RP-HPLC chromatograms. Fractions were collected, analysed by either RP-HPLC or ESI-MS, pooled and lyophilised 3 times from 10mM aq HCl.
 

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