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H<SUB>2</SUB>N-Tyr-Gly-Gly-(meta-I)Phe-Leu-OH[ No CAS ]
Yield
Reaction Conditions
Operation in experiment
55.2%
General procedure: Peptides were synthesized using a solid phase peptide synthesis protocol using an Aapptec FocusXC automated peptide synthesizer coupled with a heating system using the Fmoc chemistry andWang resin as solid support [34]. To prepare the resin for synthesis, a reaction vessel equipped with asintered glass bottom was charged with Fmoc-Leu-Wang resin (0.2 mM), and swelled in a mixture ofdichloromethane and DMF (1:1) for 15 min. The resin was then transferred to a peptide synthesizerreaction vessel. The resin was deprotected twice using 20% piperidine in DMF for 5 min at 70 C.Subsequently, an Fmoc-protected amino acid was double coupled with the Leucine-wang resin bytreating with N,N'-diisopropylcarbodiimide (3.0 equiv., 0.2 M in DMF) and Oxyma (3.0 equiv., 0.2 M inDMF) at 70 C for 8 min. Completion of coupling reactions was monitored by a Kaiser?s test for theinitial peptide [40]. Each coupling was followed by removal of the Fmoc group using 20% piperidinein DMF at 70 C for 5 min and repeated once. The cycle of the Fmoc removal and coupling wasrepeated with subsequent Fmoc-protected amino acids to generate the desired resin-bound peptide.Cleavage of the peptide from resin and concomitant deprotection of the side chain protecting groupswas carried out by shaking in TFA/triisopropylsilane/H20 (95/2.5/2.5; 5 mL), at ambient temperature for3 h. Subsequent filtration aorded the peptide in the filtrate and the volume was reduced to 0.2 mL.Then, the crude peptides were precipitated by adding cold diethyl ether, and the crude peptides werethen purified by RP-HPLC. Synthesized peptides were characterized by NMR, and the high-resolutionmass spectroscopy.
(S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-2,4-dimethylpentanoic acid[ No CAS ]
[ 84793-07-7 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-35-0 ]
[ 47375-34-8 ]
[ 94744-50-0 ]
[ 104091-08-9 ]
[ 76-05-1 ]
(S)-6-[(Diphenyl-p-tolyl-methyl)-amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid[ No CAS ]
[ 166108-71-0 ]
Fmoc-Glu(pg)-OH[ No CAS ]
Y-Aib-EGT-αMeF(2F)-TSDYSI-αMeL-LDEK((2-[2-(2-aminoethoxy)ethoxy]acetyl)2-(γGlu)-CO-(CH2)18-CO2H)AQ-Aib-EFI-(D-Glu)-YLIEGGPSSGAPPPS-NH2 trifluoroacetic acid salt[ No CAS ]
Yield
Reaction Conditions
Operation in experiment
General procedure: The peptide backbone of Peptide 1 is synthesized usingFluorenylrnethyloxycarbonyi (Fmoe)/tert-Butyl (t-Bu) chemistry on a Symphony X peptide synthesizer (Gyros Protein Technologies. Tucson, AZ).The resin consists of 1% DVB cross-linked polystyrene (Fmoc-Rink-MBHA Low Loading resin, 100-200 mesh, EMD Millipore) at a substitution of 0.3-0.4 meq/g.Standard side-chain protecting groups were used. Fmoc-Lys(Mtt)-OH is used for the lysine at position 17 and Boc-Tyr(tBu)-QH) was used for the tyrosine at position 1. Frnoc groups are removed prior to each coupling step (2 x 7 minutes) using 20% piperidine in DMF. All standard amino acid couplings are performed for 1 hour to a primary amine and 3 hour to a secondary amine, using an equal molar ratio of Fmoc amino acid (0.3 mM), diisopropyicarbodiimide (0.9 mM) and Qxyma (0.9 mM), at a 9-fold molar excess over the theoretical peptide loading. Exceptions are couplings to C -methylated amino acids, which are coupled for 3 hours. After completion of the synthesis of the peptide backbone, the resin is thoroughly washed with DCM for 6 times to remove residual DMF. The Mtt protecting group on the lysine at position 17 is selectively removed from the peptide resin using two treatments of 30% hexafuoroisopropanol (Oakwood Chemicals) in DCM (2 x 40-minute treatment).Subsequent attachment of the fatty acid-linker moiety is accomplished by coupling of 2-[2-(2-Fmoc-amino-ethoxy)-ethoxy]-acetic acid (Fmoc-AEEA-OH, ChemPep, hie.), Fmoe-glutamie acid or-t-butyl ester (Fmoc-Glu-OtBu, Ark Pharm, Inc.), eicosanedioic acid (WuXi AppTec, Shanghai, China). 3-Fold excess of reagents (AA: PyAQP: DIPEAM : 1 : 1 mol/mol) are used for each coupling that is I -hour long.After the synthesis is complete, the peptide resin is washed with DCM, and then thoroughly air-dried. The dry' resin is treated with 10 mL of cleavage cocktail(trifuoroaeetie acid: water: triisopropylsilane, 95:2,5:2.5 v/v) for 2 hours at room temperature. The resin is filtered off, washed twice each with 2 mL of neat T'FA, and the combined filtrates are treated with 5-fold excess volume of cold diethyl ether (-20C) to precipitate the crude peptide. The peptide/ether suspension is then centrifuged at 3500 rpm for 2 min to form a solid pellet, the supernatant is decanted, and the solid pellet is triturated with ether two additional times and dried in vacuo. The crude peptide is solubilized in 20% aeetonitrile/20%Acetic acid/60%water and purified by RP- HPLC on a Luna 5 /.mi Phenyl-Hexyl preparative column (21 x 250 mm, Phenomenex) with linear gradients of 100% acetonitrile and 0.1% TF A/ water buffer system (30-50% acetonitrile in 60 min). The purity of peptide is assessed using analytical RP-HPLC and pooling criteria is >95%. The main pool purity of compound 1 is found to be 98.0%. Subsequent lyophilization of the final main product pool yielded the lyophilized peptide TFA salt.The molecular weight is determined by LC- MS (obsd: M+3 =1657.2; Calc M+3=1657.0).
(S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-2,4-dimethylpentanoic acid[ No CAS ]
[ 84793-07-7 ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-35-0 ]
[ 47375-34-8 ]
[ 71989-20-3 ]
[ 94744-50-0 ]
[ 104091-08-9 ]
[ 76-05-1 ]
(S)-6-[(Diphenyl-p-tolyl-methyl)-amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid[ No CAS ]
[ 166108-71-0 ]
Y-Aib-EGT-αMeF(2F)-TSDYSI-αMeL-LDEK((2-[2-(2-aminoethoxy)ethoxy]acetyl)<SUB>2</SUB>-(γ-Glu)-CO-(CH2)<SUB>18</SUB>-CO<SUB>2</SUB>H)AQ-Aib-EFI-(D-Glu)-YLIEGGPSSGAPPPS-NH<SUB>2</SUB><SUB> trifluoroacetic acid salt</SUB>[ No CAS ]
Yield
Reaction Conditions
Operation in experiment
The peptide backbone of Example 1 is synthesized using Fluorenylmethyloxycarbonyl (Fmoc)/tert-Butyl (t-Bu) chemistry on a Symphony X peptide synthesizer (Gyros Protein Technologies. Tucson, Ariz.). The resin consists of 1% DVB cross-linked polystyrene (Fmoc-Rink-MBHA Low Loading resin, 100-200 mesh, EMD Millipore) at a substitution of 0.3-0.4 meq/g. Standard side-chain protecting groups were used. Fmoc-Lys(Mtt)-OH is used for the lysine at position 17 and Boc-Tyr(tBu)-OH) was used for the tyrosine at position 1. Fmoc groups are removed prior to each coupling step (2×7 minutes) using 20% piperidine in DMF. All standard amino acid couplings are performed for 1 hour to a primary amine and 3 hour to a secondary amine, using an equal molar ratio of Fmoc amino acid (0.3 mM), diisopropylcarbodiimide (0.9 mM) and Oxyma (0.9 mM), at a 9-fold molar excess over the theoretical peptide loading. Exceptions are couplings to Calpha-methylated amino acids, which are coupled for 3 hours. After completion of the synthesis of the peptide backbone, the resin is thoroughly washed with DCM for 6 times to remove residual DMF. The Mtt protecting group on the lysine at position 17 is selectively removed from the peptide resin using two treatments of 300 hexafluoroisopropanol (Oakwood Chemicals) in DCM (2×40-minute treatment). Subsequent attachment of the fatty acid-linker moiety is accomplished by coupling of 2-[2-(2-Fmoc-amino-ethoxy)-ethoxy]-acetic acid (Fmoc-AEEA-OH, ChemPep, Inc.), Fmoc-glutamic acid alpha-t-butyl ester (Fmoc-Glu-OtBu, Ark Pharm, Inc.), mono-OtBu-eicosanedioic acid (WuXi AppTec, Shanghai, China). 3-Fold excess of reagents (AA:PyAOP:DIPEA=1:1:1 mol/mol) are used for each coupling that is 1-hour long. After the synthesis is complete, the peptide resin is washed with DCM, and then thoroughly air-dried. The dry resin is treated with 10 mL of cleavage cocktail (trifluoroacetic acid:water:triisopropylsilane, 95:2.5:2.5 v/v) for 2 hours at room temperature. The resin is filtered off, washed twice each with 2 mL of neat TFA, and the combined filtrates are treated with 5-fold excess volume of cold diethyl ether (-20 C.) to precipitate the crude peptide. The peptide/ether suspension is then centrifuged at 3500 rpm for 2 min to form a solid pellet, the supernatant is decanted, and the solid pellet is triturated with ether two additional times and dried in vacuo. The crude peptide is solubilized in 20% acetonitrile/20% Acetic acid/60% water and purified by RP-HPLC on a Luna 5 mum Phenyl-Hexyl preparative column (21*250 mm, Phenomenex) with linear gradients of 100% acetonitrile and 0.1% TFA/water buffer system (30-50% acetonitrile in 60 min). The purity of peptide is assessed using analytical RP-HPLC and pooling criteria is >95%. The main pool purity of compound 1 is found to be 98.0%. Subsequent lyophilization of the final main product pool yielded the lyophilized peptide TFA salt. The molecular weight is determined by LC-MS (obsd. M+3=1657.2; Calc M+3=1657.0).
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