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

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

Document Type: Review Article


Affiliations: IPF PharmaCeuticals GmbH, Feodor-Lynen Strasse 31, 30625 Hannover, Germany.

Publication date: December 1, 2004

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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