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2-chlorotrityl chloride polystyrene resin[ No CAS ]
[ 162502-65-0 ]
[ 27144-18-9 ]
[ 29022-11-5 ]
[ 71989-31-6 ]
[ 71989-23-6 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 86060-81-3 ]
[ 109425-55-0 ]
C93H116N11O16PolS2[ No CAS ]
Yield
Reaction Conditions
Operation in experiment
Synthesis of the peptide is carried out by a regular stepwise Fmoc SPPS procedure starting from 2-Cl-Trt-chloride resin. The first amino acid (Fmoc-Gly) is loaded on the resin as described in previous examples to obtain a loading of about 0.7 mmol/g of amino acid/resin. After washing of the resin and removal of the Fmoc group by treatment with piperidine/DMF, the second amino acid (Fmoc-Orn(Boc)) is introduced to continue sequence elongation. Fmoc protected amino acids are activated in situ using TBTU/HOBt and subsequently coupled to the resin over about 50 minutes. Diisopropylethylamine or collidine is used during coupling as an organic base. Completion of the coupling is indicated by ninhydrin test. After washing of the resin, the Fmoc protecting group on the alpha-amine is removed with 20% piperidine in DMF for 20 min. These steps are repeated each time with another amino acid according to the peptide sequence. All amino acids used are Fmoc-Nalpha protected. Trifunctional amino acids are side chain protected as follows: Cys(Acm), Thr(tBu), Asn(Trt), and Orn(Boc). Three equivalents of the activated amino acids are used in the coupling reactions. At the end of the synthesis, the peptide-resin is washed with DMF, followed by DCM, and dried under vacuum to obtain dry peptide-resin.
Chelmical synthesis: Peptides were synthesized on a Rink amide resin, 0.45 mmol/g [Fmoc-Cys(Trityl)-Wang; Novabiochem, San Diego, Calif.] usinig N-(9-fluorenyl)methoxycarboxyl chemistry and standard side chain protection except on cysteine residues. Cysteine residues were protected in pairs with either S-trityl on the first and third cysteines or S-acetamidomethyl on the second and fourth cysteines. Amino acid derivatives were from Advanced Chemtech (Louisville, Ky.). The peptides were removed from the resin and precipitated, and a two-step oxidation protocol was used to selectively fold the peptides as described previously (Luo et al., 1999). Briefly, the first disulfide bridge was closed by dripping the peptide into an equal volume of 20 mM potassium feliicyanide and 0.1 M Tris, pH 7.5. The solution was allowed to react for 30 min, and the monocyclic peptide was purified by reverse-phase HPLC. Simultaneous removal of the S-acetamidomethyl groups and closure of the second disulfide bridge was carried out by iodine oxidation. The monocyclic peptide and HPLC eluent was dripped into an equal volume of iodine (10 mM) in H20/trifluoroacetic acid/acetonitrile (78:2:20 by volume) and allowed to react for 10 min. The reaction was terminated by the addition of ascorbic acid diluted 20-fold with 0.1percent trifluoroacetic acid and the bicyclic product purified by HPLC. Mass Spectrometry: Measurements were performed at the Salk Institute for Biological Studies (San Diego, Calif.) under the direction of Jean Rivier. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry and liquid secondary ionization mass spectrometry were used.
N-alpha-Fmoc-N-beta-O-t-butyl-L-aspartyl-N-α-(2,4-dimethoxybenzyl)glycine[ No CAS ]
[ 29022-11-5 ]
[ 68858-20-8 ]
[ 35661-60-0 ]
[ 13734-34-4 ]
[ 957780-56-2 ]
[ 35661-39-3 ]
[ 920519-33-1 ]
(2S)-N-((9H-fluoren-9-ylmethyloxy)carbonyl)aspartic acid-4-((3-ethyl)pent-3-yl) ester[ No CAS ]
Fmoc-Gly-Ser(ψMe,MePro)-OH[ No CAS ]
Fmoc-Gln(Trt)-Thr(ψMe,MePro)-OH[ No CAS ]
[ 71989-31-6 ]
[ 35661-40-6 ]
[ 71989-33-8 ]
[ 71989-14-5 ]
[ 71989-18-9 ]
[ 71989-23-6 ]
[ 71989-38-3 ]
[ 71989-26-9 ]
[ 103213-32-7 ]
[ 71989-35-0 ]
[ 132388-59-1 ]
[ 132327-80-1 ]
[ 86060-81-3 ]
[ 109425-51-6 ]
[ 77284-32-3 ]
Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine[ No CAS ]
[Cys105,Nle125,170,Cys(Acm)165,182,189,Asn107,Asp109](105-191)hGH-NH2[ No CAS ]
Yield
Reaction Conditions
Operation in experiment
101.1 mg
General procedure: The syntheses of the fragments were performed on an automatic peptide synthesizer under microwave conditions using an 8-fold excess of 0.5 M amino acids, 0.5 M HATU/NMP, 2 M DIEA /NMP or 1.0 M DIC/NMP and 0.5 M Oxyma /NMP. The final concentration of Fmoc-amino acids was 0.2 M. The coupling cycles were conducted according to Table 1. Fmoc deprotection was carried out using 35% piperidine/NMP containing 0.1 M HOBt at room temperature for 2 and 6 min, followed by 4 min at 48 C.
Chemistry
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