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A Synthetic Approach to a Peptide α‐Thioester from an Unprotected Peptide through Cleavage and Activation of a Specific Peptide Bond by N ‐Acetylguanidine
Author(s) -
Okamoto Ryo,
Morooka Keiko,
Kajihara Yasuhiro
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201105601
Subject(s) - thioester , peptide , cleavage (geology) , peptide bond , chemistry , cysteine , combinatorial chemistry , native chemical ligation , residue (chemistry) , stereochemistry , biochemistry , biology , enzyme , paleontology , fracture (geology)
A different route to peptide α‐thioesters through a new peptide‐bond‐cleavage method at a cysteine residue by S‐thiocarbonylation and subsequent treatment with N ‐acetylguanidine is described (see scheme). The resultant peptidyl‐ N ‐acetylguanidine can be converted into the corresponding peptide α‐thioester and is also usable as an alternative to a peptide α‐thioester. This method allows efficient kinetically controlled ligation in the presence of thiols.