Traceless synthesis of protein thioesters using enzyme-mediated hydrazinolysis and subsequent self-editing of the cysteinyl prolyl sequence

A traceless thioester-producing protocol featuring carboxypeptidase Y-mediated hydrazinolysis of cysteinyl prolyl leucine-tagged peptides has been developed. The hydrazinolysis followed by thioesterification affords cysteinyl prolyl thioesters. Self-editing of the tag and subsequent trans -thioester...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2019-06, Vol.55 (49), p.729-732
Main Authors: Komiya, Chiaki, Shigenaga, Akira, Tsukimoto, Jun, Ueda, Masahiro, Morisaki, Takuya, Inokuma, Tsubasa, Itoh, Kohji, Otaka, Akira
Format: Article
Language:English
Subjects:
Carboxypeptidases - metabolism
Cysteine - chemistry
Cysteine - metabolism
Editing
Esters - chemistry
Esters - metabolism
Hydrazines - chemistry
Hydrazines - metabolism
Leucine
Molecular Conformation
Peptides
Proteins
Sulfhydryl Compounds - chemistry
Sulfhydryl Compounds - metabolism
Thioesterification
Thioesters
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Summary:A traceless thioester-producing protocol featuring carboxypeptidase Y-mediated hydrazinolysis of cysteinyl prolyl leucine-tagged peptides has been developed. The hydrazinolysis followed by thioesterification affords cysteinyl prolyl thioesters. Self-editing of the tag and subsequent trans -thioesterification yields peptide thioesters. The developed protocol was successfully applied to the conversion of recombinant proteins to thioesters. Thioester-producing protocol featuring carboxypeptidase Y (CPaseY)-mediated hydrazinolysis and subsequent self-editing of tag affords protein thioesters in a traceless manner.
ISSN:1359-7345
1364-548X
DOI:10.1039/c9cc03583d