期刊
JOURNAL OF PEPTIDE SCIENCE
卷 20, 期 2, 页码 92-97出版社
WILEY-BLACKWELL
DOI: 10.1002/psc.2580
关键词
bis(2-sulfanylethyl)amido (SEA); thioester; Fmoc-SPPS; thiol exchange
Protein total chemical synthesis enables the atom-by-atom control of the protein structure and therefore has a great potential for studying protein function. Native chemical ligation of C-terminal peptide thioesters with N-terminal cysteinyl peptides and related methodologies are central to the field of protein total synthesis. Consequently, methods enabling the facile synthesis of peptide thioesters using Fmoc-SPPS are of great value. Herein, we provide a detailed protocol for the preparation of bis(2-sulfanylethyl)amino polystyrene resin as a starting point for the synthesis of C-terminal bis(2-sulfanylethyl)amido peptides and of peptide thioesters derived from 3-mercaptopropionic acid. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd.
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