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Issue 23, 2014
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Development and application of serine/threonine ligation for synthetic protein chemistry

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Abstract

Chemical synthesis of proteins, especially those with post-translational modifications, has offered new opportunities to study the protein structure–function relationship. In the past four years, we have developed the serine/threonine ligation (STL), which involves the chemoselective reaction between peptide salicylaldehyde esters and peptides with N-terminal serine or threonine. The method has been successfully applied to the synthesis of both linear and cyclic peptides/proteins.

Graphical abstract: Development and application of serine/threonine ligation for synthetic protein chemistry

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Publication details

The article was received on 20 Feb 2014, accepted on 09 Apr 2014 and first published on 10 Apr 2014


Article type: Perspective
DOI: 10.1039/C4OB00392F
Author version available: Download Author version (PDF)
Citation: Org. Biomol. Chem., 2014,12, 3768-3773
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    Development and application of serine/threonine ligation for synthetic protein chemistry

    H. Liu and X. Li, Org. Biomol. Chem., 2014, 12, 3768
    DOI: 10.1039/C4OB00392F

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