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Native chemical ligation of hydrophobic peptides in organic solvents
Author(s) -
Dittmann Marc,
Sauermann Jörg,
Seidel Ralf,
Zimmermann Wolfgang,
Engelhard Martin
Publication year - 2010
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1285
Subject(s) - native chemical ligation , chemistry , ligation , chemical ligation , combinatorial chemistry , organic chemistry , peptide , biochemistry , cysteine , biology , microbiology and biotechnology , enzyme
The application of chemistry to hydrophobic peptides and membrane‐spanning helices is hampered by the fact that they are only poorly soluble in aqueous buffers and that they have a tendency for aggregation. These properties lead to difficulties when purifying them after chemical synthesis and particularly interfere with native chemical ligation. Here, we describe native chemical ligation of model peptides in the organic solvent dimethylformamide (DMF) under anhydrous conditions. Best results concerning yields and complete solubility are obtained if thiophenole is used in the presence of LiCl. These conditions might be applicable also for the ligation of transmembrane helices. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.