Formation of aminosuccinyl derivative from β-phenacyl aspartyl peptides catalyzed by sodium thiophenoxide
| Autor: | Pierrette Gaudreau, John L. Morell, Erhard Gross |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
chemistry.chemical_classification
Chemistry Sodium Side reaction chemistry.chemical_element Succinates Peptide Phenacyl Biochemistry Medicinal chemistry Tetragastrin Amino acid Residue (chemistry) chemistry.chemical_compound stomatognathic system Amide Reagent Gastrins Methods Solvents Organic chemistry Indicators and Reagents Amino Acids Countercurrent Distribution Oligopeptides |
| Zdroj: | International Journal of Peptide and Protein Research. 19:280-283 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1982.tb03039.x |
| Popis: | In the solid-phase synthesis of cholecystokinin 30-33, Trp-Met-Asp-Phe- amide, the beta-phenacyl ester was used to protect the beta-carboxyl of aspartyl residue. The ester was cleaved, on the solid support, with a 1 M solution of sodium thiophenoxide in DMF, prior to ammonolysis. The product, after purification by countercurrent distribution, was identified as a mixture of isoasparaginyl and aspartyl peptides. A study of the deprotection step, with sodium thiophenoxide, on a model peptide (t-butyloxycarbonyl-beta-phenacyl-aspartyl-phenylalanineamide) showed the rapid formation of the aminosuccinyl derivative, catalyzed by this reagent. |
| Databáze: | OpenAIRE |
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