Stability and cleavage conditions of (2-furyl)-L-alanine-containing peptides.
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.
Schulz
Axel
A
IPF PharmaCeuticals GmbH, Feodor-Lynen Strasse 31, 30625 Hannover, Germany. a.schulz@ipf-pharmaceuticals.de
Busmann
Annette
A
Klüver
Enno
E
Schnebel
Matthias
M
Adermann
Knut
K
D000409:Alanine / Q000031:analogs & derivatives*; D002851:Chromatography, High Pressure Liquid; D005019:Ethyl Ethers / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism*; D012821:Silanes / Q000378:metabolism; D013438:Sulfhydryl Compounds / Q000378:metabolism; D014269:Trifluoroacetic Acid
C471080:3,6-dioxa-1,8-octanedithiol; D005019:Ethyl Ethers; D010446:Peptide Fragments; D012821:Silanes; D013438:Sulfhydryl Compounds; D014269:Trifluoroacetic Acid; D000409:Alanine