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

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

Volume: 11 Issue: 6

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

Affiliation:

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

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.

Cite this article as:

Schulz Axel, Busmann Annette, Kluver Enno, Schnebel Matthias and Adermann Knut, Stability and Cleavage Conditions of (2-Furyl)-L-Alanine-Containing Peptides, Protein & Peptide Letters 2004; 11 (6) . https://dx.doi.org/10.2174/0929866043406238