title: Native chemical ligation of hydrophobic peptides in organic solvents.
abstract: 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.
authors.affiliation: Max Planck Institute of Molecular Physiology, Dortmund, Germany.
authors.forename: Marc
authors.initials: M
authors.lastname: Dittmann
authors.forename: Jörg
authors.initials: J
authors.lastname: Sauermann
authors.forename: Ralf
authors.initials: R
authors.lastname: Seidel
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Zimmermann
authors.forename: Martin
authors.initials: M
authors.lastname: Engelhard
mesh_terms: D004126:Dimethylformamide / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry*; D014867:Water / Q000737:chemistry
chemical_list: D010455:Peptides; D012997:Solvents; D014867:Water; D004126:Dimethylformamide