Stability and Cleavage Conditions of (2-Furyl)-L-Alanine-Containing Peptides

Author(s): Axel Schulz, Annette Busmann, Enno Kluver, Matthias Schnebel, Knut Adermann.

Journal Name: Protein & Peptide Letters

Volume 11 , Issue 6 , 2004

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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.

Keywords: peptide synthesis, scavenger, thiol, (2-furyl)-l-alanine, cleavage, dithioacetale

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Article Details

VOLUME: 11
ISSUE: 6
Year: 2004
Page: [601 - 606]
Pages: 6
DOI: 10.2174/0929866043406238
Price: $65

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