Two-step hard acid deprotection/cleavage procedure for solid phase peptide synthesis
| Autor: | Ako Ohkubo, Nobutaka Fujii, Yoshimasa Inagaki, Akira Otaka, Peter P. Roller, Motoyoshi Nomizu, Takeyoshi Yamashita, Haruaki Yajima |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Trimethylsilyl Compounds
Chemical Phenomena Formic Acid Esters Urotensins Molecular Sequence Data Peptide Biochemistry chemistry.chemical_compound Trimethylsilyl trifluoromethanesulfonate Acetamides Peptide synthesis Trifluoroacetic acid Humans Trifluoroacetic Acid Moiety Organic chemistry Amino Acid Sequence Peptide sequence Chromatography High Pressure Liquid Bond cleavage Phenylacetates chemistry.chemical_classification Endothelins Thioanisole Tryptophan Combinatorial chemistry Chemistry chemistry Indicators and Reagents Peptides Resins Plant |
| Zdroj: | International Journal of Peptide and Protein Research. 37:145-152 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1991.tb00095.x |
| Popis: | A new two-step deprotection/cleavage procedure for t-butoxycarbonyl (Boc) based solid phase peptide synthesis is reported. First the protective groups are removed from 4-(oxymethyl)-phenylacetamidomethyl (PAM) resin attached peptide with the weak hard acid, trimethylsilyl bromide-thioanisole/trifluoroacetic acid (TFA). In the second step, the peptide is cleaved from the resin with a stronger hard acid such as trimethylsilyl trifluoromethanesulfonate in TFA or with HF. The method is also shown to deformylate Nin-formyltryptophan moiety efficiently. The usefulness of this procedure for practical solid phase peptide synthesis is demonstrated by comparison with other deprotection methods in the synthesis of urotensin II and human endothelin. |
| Databáze: | OpenAIRE |
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