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The Mercaptomethyl Group Facilitates an Efficient One‐Pot Ligation at Xaa‐Ser/Thr for (Glyco)peptide Synthesis
Author(s) -
Hojo Hironobu,
Ozawa Chinatsu,
Katayama Hidekazu,
Ueki Akiharu,
Nakahara Yuko,
Nakahara Yoshiaki
Publication year - 2010
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.201000384
Subject(s) - ligation , peptide , group (periodic table) , peptide synthesis , chemical ligation , combinatorial chemistry , chemistry , medicine , biochemistry , computer science , organic chemistry
Going native : A mercaptomethyl group on the side‐chain hydroxy group of serine and threonine residues facilitates a native chemical ligation reaction at the Xaa‐Ser/Thr site (see scheme; R=H or Me). The intermediate thioester is treated to achieve an S ‐ to N ‐acyl shift. After ligation, the group is spontaneously removed to obtain the glycopeptide contulakin‐G and human calcitonin.

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