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New semi-synthesis of ubiquitin C-terminal conjugate with 7-amino-4-methylcoumarin

The ligation of peptide hydrazides at a Gly site carrying a removal auxiliary was found to be an efficient process. This technology was successfully used for the synthesis of ubiquitin C‐terminal conjugates. Recombinant Ub(1–75)‐NHNH2 was prepared through the hydrozinolysis of the Ub(1–75)‐intein fu...

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Bibliographic Details
Published in:Journal of peptide science 2014-02, Vol.20 (2), p.102-107
Main Authors: Li, Yi-Tong, Liang, Jun, Li, Jia-Bin, Fang, Ge-Min, Huang, Yong, Liu, Lei
Format: Article
Language:English
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Summary:The ligation of peptide hydrazides at a Gly site carrying a removal auxiliary was found to be an efficient process. This technology was successfully used for the synthesis of ubiquitin C‐terminal conjugates. Recombinant Ub(1–75)‐NHNH2 was prepared through the hydrozinolysis of the Ub(1–75)‐intein fusion protein. It was ligated with a glycine derivative modified with an acid‐sensitive thiol auxiliary. The final acid treatment produced the desired bioactive ubiquitin conjugates in practical quantities. Thus, the method described here extends the protocols of expressed protein ligation. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd. Native chemical ligation of a recombinant peptide hydrazide with a Gly‐peptide carrying a removal auxiliary was examined and used to synthesize ubiquitin C‐terminal conjugates.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.2568