Home Cart Sign in  
Chemical Structure| 1315449-94-5 Chemical Structure| 1315449-94-5

Structure of Fmoc-α-Me-D-Lys(Boc)-OH
CAS No.: 1315449-94-5

Chemical Structure| 1315449-94-5

*Storage: {[sel_prStorage]}

*Shipping: {[sel_prShipping]}

,{[proInfo.pro_purity]}

4.5 *For Research Use Only !

{[proInfo.pro_purity]}
Cat. No.: {[proInfo.prAm]} Purity: {[proInfo.pro_purity]}

Change View

Size Price VIP Price

US Stock

Global Stock

In Stock
{[ item.pr_size ]} Inquiry {[ getRatePrice(item.pr_usd,item.pr_rate,item.mem_rate,item.pr_is_large_size_no_price, item.vip_usd) ]}

US Stock: ship in 0-1 business day
Global Stock: ship in 5-7 days

  • {[ item.pr_size ]}

In Stock

- +

Please Login or Create an Account to: See VIP prices and availability

US Stock: ship in 0-1 business day
Global Stock: ship in 2 weeks

  • 1-2 Day Shipping
  • High Quality
  • Technical Support
Product Citations

Alternative Products

Product Details of [ 1315449-94-5 ]

CAS No. :1315449-94-5
Formula : C27H34N2O6
M.W : 482.57
SMILES Code : O=C(O)[C@](C)(NC(OCC1C2=C(C3=C1C=CC=C3)C=CC=C2)=O)CCCCNC(OC(C)(C)C)=O
MDL No. :MFCD17019260
InChI Key :MYQXEVZHWDILHG-HHHXNRCGSA-N
Pubchem ID :75534968

Safety of [ 1315449-94-5 ]

GHS Pictogram:
Signal Word:Warning
Hazard Statements:H315-H319-H335
Precautionary Statements:P261-P305+P351+P338

Application In Synthesis of [ 1315449-94-5 ]

* 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 [ 1315449-94-5 ]

[ 1315449-94-5 ] Synthesis Path-Downstream   1~11

  • 1
  • [ 17377-68-3 ]
  • [ 1315449-94-5 ]
  • 2
  • [ 1453179-18-4 ]
  • [ 1315449-94-5 ]
  • 3
  • [ 1453178-54-5 ]
  • [ 1315449-94-5 ]
  • 4
  • [ 1453178-56-7 ]
  • [ 1315449-94-5 ]
  • 5
  • [ 1453178-58-9 ]
  • [ 1315449-94-5 ]
  • 6
  • [ 1453178-60-3 ]
  • [ 1315449-94-5 ]
  • 7
  • [ 1453178-62-5 ]
  • [ 1315449-94-5 ]
  • 8
  • [ 24424-99-5 ]
  • C22H26N2O4 [ No CAS ]
  • [ 1315449-94-5 ]
  • 9
  • C17H30N2O5 [ No CAS ]
  • [ 1315449-94-5 ]
  • 10
  • [ 29022-11-5 ]
  • [ 68858-20-8 ]
  • [ 35661-60-0 ]
  • [ 35661-39-3 ]
  • [ 1315449-94-5 ]
  • [ 71989-31-6 ]
  • [ 35661-40-6 ]
  • [ 71989-33-8 ]
  • [ 71989-14-5 ]
  • [ 71989-18-9 ]
  • [ 71989-23-6 ]
  • [ 71989-38-3 ]
  • [ 71989-26-9 ]
  • [ 71989-35-0 ]
  • [ 132327-80-1 ]
  • [ 94744-50-0 ]
  • [ 143824-78-6 ]
  • Y-Aib-E-G-T-F-T-S-D-L-S-I-Q-L-E-E-E-A-V-(R)MeLys-L-F-I-E-W-L-K-A-G-G-P-S-S-G-A-P-P-P-S-NH2 [ No CAS ]
YieldReaction ConditionsOperation in experiment
General procedure: Example 1 Synthesis of SEQ ID NO: 10 (0298) The solid phase synthesis was carried out on Rink-resin with a loading of 0.29 mmol/g, 75-150 mum from the company Agilent Technologies. The Fmoc-synthesis strategy was applied with HBTU/DIPEA-activation. The peptide was cleaved from the resin with King's cocktail (D. S. King, C. G. Fields, G. B. Fields, Int. J. Peptide Protein Res. 36, 1990, 255-266). The crude product was purified via preparative HPLC on a Waters column (XBridge, BEH130, Prep C18 5 muM) using an acetonitrile/water gradient (both buffers with 0.1% TFA). The purified peptide was analysed by LCMS (Method C4). Deconvolution of the mass signals found under the peak with retention time 9.55 min revealed the peptide mass 4164.1 which is in line with the expected value of 4163.7 The solid phase peptide syntheses were performed for example on a Prelude Peptide Synthesizer (Protein Technologies Inc) or similar automated synthesizer using standard Fmoc chemistry and HBTU/DIPEA activation. DMF was used as the solvent. Deprotection: 20% piperidine/DMF for 2×2.5 min. Washes: 7×DMF. Coupling 2:5:10 200 mM AA/500 mM HBTU/2M DIPEA in DMF 2× for 20 min. Washes: 5×DMF. (0251) All the peptides that had been synthesized were cleaved from the resin with King's cleavage cocktail consisting of 82.5% TFA, 5% phenol, 5% water, 5% thioanisole, 2.5% EDT. The crude peptides were then precipitated in diethyl or diisopropyl ether, centrifuged, and lyophilized. Peptides were analyzed by analytical HPLC and checked by ESI mass spectrometry. Crude peptides were purified by a conventional preparative HPLC purification procedure.
  • 11
  • Fmoc-Rink resin [ No CAS ]
  • [ 29022-11-5 ]
  • [ 68858-20-8 ]
  • [ 35661-60-0 ]
  • [ 35661-39-3 ]
  • [ 1315449-94-5 ]
  • [ 35661-40-6 ]
  • [ 71989-33-8 ]
  • [ 71989-18-9 ]
  • [ 108-24-7 ]
  • [ 71989-23-6 ]
  • [ 71989-26-9 ]
  • [ 71989-35-0 ]
  • [ 94744-50-0 ]
  • [ 150629-67-7 ]
  • [ 159766-56-0 ]
  • Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine [ No CAS ]
  • Ac-L-E(OtBu)-G-R(Pfb)-E(OtBu)-K(Boc)-V-R(Pfb)-A-K(Ac)-I-Aib-Aib-E(OtBu)-G-K(Dde)-S(tBu)-T(tBu)-F-S(tBu)-Mly(Boc)-R(Pfb)-A-K(Ac)-NH-Rink Amide Resin, Ac - acetyl, Aib - 2-amino-isobutyric acid, Boc - tert-butyloxycarbonyl, Dde - 1-(4,4-dimethyl-2,6-dioxocyclohex-1-ylidene)ethyl, Mly - α-methyl-lysine, Pfb - 2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl, tBu - tert-butyl [ No CAS ]
YieldReaction ConditionsOperation in experiment
2.A Loading of Fmoc-Lys(Ac)-OH on Rink Amide Resin (0433) In a 100 ml reactor equipped with a sintered glass at the bottom, 6 g of Novabiochem or ChemImpex Rink amide AM resin (Low Loading 0.47 mmol/g) was swelled in 40 ml of DMF. The solvent was drained and 30 ml of 20% piperidine in DMF solution were added. After 15 min shaking, the solvent was drained. This was repeated twice to ensure complete Fmoc protecting group removal. The resin was washed with 5×30 ml DMF. (0434) In a separate flask a solution containing Fmoc-Lys(Ac)-OH (3.5 g, 8 mmol, 3 eq.) HOBT.H2O (1.3 g 8.5 mmol) in 30 ml DMF was prepared. Diisopropylcarbodiimide (DIC) (1 g, 8.5 mmol) was added to this solution and after 5 min the resulting mixture was added to the resin. The suspension was shaken on a stirring plate for 4 h or until completion of the reaction as judged by Kaiser Test (Ninhidrin test) on an aliquot part of the resin. (0435) The solvent was then drained and the resin washed 3 times with 30 ml DMF. Fmoc-Lys(Ac)-NH2 loaded resin was used immediately for subsequent steps or stored wet at 4 C. until needed. (0436) 2.B. Synthesis of Peptide Having the SEQ ID NO: 3 (0437) The following synthesis was performed using 5 times an amount of resin obtained at step 2.A. corresponding to 0.2 mmol of Fmoc-Lys(Ac)-NH2 each. The syntheses were performed separately on each individual batches using a CEM Liberty Blue microwave peptide synthesizer to assemble the second and third residue of the peptide sequence (starting from the C-terminus). (0438) Peptide synthesis was performed by using DIC 0.5M/Oxyma 1M in DMF. (0439) All amino acids were introduced with double couplings using standard heating protocol. (0440) The resin was removed from the synthesizer and Fmoc-alpha-methyl-lysine(Boc)-OH (3 eq.) was coupled manually using 3 eq. Oxyma and 3 eq. DIC with microwave heating (75 C. 15 sec. and 90 C. 110 sec). The completion of the reaction was controlled by Kaiser test. If positive, DIC 3 eq. was added followed by microwave heating as above. When coupling of Fmoc-alpha-methyl-lysine(Boc)-OH was complete the rest of the peptide sequence was assembled using a CEM Liberty Blue microwave peptide synthesizer. (0442) All amino acids were introduced with double couplings at 90 C. as above, with the exception of amino-isobutyric acid at position 21 and serine at position 29 for which a triple coupling at 90 for 2 minutes was performed. Fmoc-Lys(Dde)-OH was used at position 25. (0443) At the end of the 5 syntheses, the 5 batches of resin were combined and transferred into a 50 mL polypropylene syringe and the peptide was acetylated at N-terminus with acetic anhydride (944 10 mmol) in DMF (30 mL) for 20 minutes, repeating the cycle twice. (0444) Then, Dde protecting group on Lysine 25 side chain was removed by percolating 50 mL of a solution of hydrazine 5% w/v in DMF, followed by DMF washes (5×20 ml). The reaction was monitored by Kaiser Test and cleavage of an aliquot part of resin and UPLC/MS analysis. (0445) Three TTDS spacer units were introduced by single coupling by performing three times the following procedure: To the resin a solution of Fmoc-TTDS-OH (1.62 g, 3 mmol) in 30 mL of DMF were added followed by HOAt (5 ml of a 0.6 ml solution in DMF, 3 mmol) and DIC (1 ml, 6 mmol). The syringe was agitated on an orbital table for 18 h. The reaction was monitored by Kaiser Test. The resin was washed with DMF (2×30 mL). Then to the resin, 30 mL of 20% v/v of piperidine in DMF was added. The syringe was agitated on an orbital table for 20 min. This deprotection procedure was repeated a second time and the resin was washed with DMF (2×30 mL) and dichloromethane (3×30 mL). (0446) The three gamma-glutamic acids spacers were introduced by performing a double coupling of each Fmoc-Glu-OtBu. Thus the following procedure was applied three times: To the resin a solution (4S)-5-tert-butoxy-4-(9H-fluoren-9-yl methoxy carbonylamino)-5-oxo-pentanoic acid (Fmoc-Glu-OtBu) (1.275 g, 3 mmol) in of 30 mL of DMF were added followed by HOAt (5 ml of a 0.6 ml solution in DMF 3 mmol) and DIC (1 ml, 6 mmol). The syringe was agitated on an orbital table for 4 h. The resin was washed with DMF (2×20 mL) and the coupling was repeated a second time. The reaction was monitored by Kaiser Test. The resin was washed with DMF (2×30 mL). Then to the resin, 30 mL of 20% v/v of piperidine in DMF was added. The syringe was agitated on an orbital table for 20 min. This deprotection procedure was repeated a second time and the resin was washed with DMF (3×30 mL) and dichloromethane (3×30 mL). (0448) Finally, the peptide was acylated with palmitic acid (768 mg, 3 mmol), HOAt (5 ml of a 0.6 M solution in DMF, 3 mmol) and DIC (1 ml, 6 mmol) activation in DMF (30 mL) for 2.5 h. The resin was washed with DMF (2×30 mL) and dichloromethane (3×30mL) and dried under vacuum. (0449) The cleavage of the peptide from the resin was performed using a solution phenol (6.25 g), water (6.25 mL) and TIPS (3 mL) ...
 

Historical Records

Technical Information

Categories