Native chemical ligation derived method for recombinant peptide/protein C-terminal amidation.

C-terminal amidation is often a requisite structural feature for peptide hormone bio-activity. We report a chemical amidation method that converts peptide/protein thioesters into their corresponding C-terminal amides. The peptide/protein thioester is treated with 1-(2,4-dimethoxyphenyl)-2-mercaptoethyl auxiliary (1b) in a native chemical ligation (NCL) reaction to form an intermediate, which upon removal of the auxiliary with TFA, yields the peptide/protein amide. We have demonstrated the general utility of the approach by successfully converting several synthetic peptide thioesters to peptide amides with high conversion rates. Preliminary results of converting a recombinant peptide thioester to its amide form are also reported. Copyright © 2013 Elsevier Ltd. All rights reserved.

Citation

Chengzao Sun, Gary Luo, Swetha Neravetla, Soumitra S Ghosh, Bruce Forood. Native chemical ligation derived method for recombinant peptide/protein C-terminal amidation. Bioorganic & medicinal chemistry letters. 2013 Sep 15;23(18):5203-8

PMID: 23880540

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