期刊
JOURNAL OF PEPTIDE SCIENCE
卷 16, 期 10, 页码 558-562出版社
WILEY
DOI: 10.1002/psc.1285
关键词
ligation in organic solvents; transmembrane proteins; peptide synthesis; hydrophobic peptides
资金
- Volkswagenstiftung
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 LiCI. These conditions might be applicable also for the ligation of transmembrane helices. Copyright (C) 2010 European Peptide Society and John Wiley & Sons, Ltd.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据