1. Stability and cleavage conditions of (2-furyl)-L-alanine-containing peptides.
- Author
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Schulz A, Busmann A, Klüver E, Schnebel M, and Adermann K
- Subjects
- Chromatography, High Pressure Liquid, Ethyl Ethers metabolism, Silanes metabolism, Sulfhydryl Compounds metabolism, Trifluoroacetic Acid, Alanine analogs & derivatives, Peptide Fragments metabolism
- Abstract
The furyl group of (2-furyl)-L-alanine-containing peptides obtained from Fmoc solid-phase synthesis is partially degraded to several by-products during the final TFA-mediated deprotection in the presence of cation scavengers such as ethanedithiol and propanedithiol. The major by-product corresponds to a bis-dithioacetale formed after acidic hydrolysis of the furyl group. We examined several cleavage conditions and found that cleavage cocktails containing water and triisopropylsilane or 3,6-dioxa-1,8-octanedithiol (DODT) in trifluoroacetic acid are sufficient to minimize the side reaction.
- Published
- 2004
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