| Autor: |
Theodore Lambros, M Waki, Chi-Deu Chang, Raymond Makofske, Johannes Meienhofer, Edgar P. Heimer |
| Rok vydání: |
2009 |
| Předmět: |
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| Zdroj: |
International Journal of Peptide and Protein Research. 13:35-42 |
| ISSN: |
0367-8377 |
| DOI: |
10.1111/j.1399-3011.1979.tb01847.x |
| Popis: |
The utility of repetitive nonhydrolytic base cleavage of alpha-amino protective groups in solid phase peptide synthesis is shown by a preparation of the model tetrapeptide leucyl-alanyl-glycyl-valine on a p-benzyloxybenzyl ester polystyrene--1% divinylbenzene resin support. Nalpha-9-Fluorenylmethyloxycarbonyl (Fmoc: Carpino & Han, 1970, 1972) amino acids were coupled by the symmetrical anhydride procedure, followed by Fmoc group cleavage using 50% piperidine in methylene chloride. Quantitative removal of the Fmoc-tetrapeptide from the solid support was effected by treatment with 55% trifluoroacetic acid in methylene chloride. Homogeneous free tetrapeptide was obtained in 87% overall yield. The procedure is proposed to offer advantages over present solid phase methods which use acidolysis for repetitive alpha-amino group deblocking. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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