Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10595136 | Bioorganic & Medicinal Chemistry Letters | 2013 | 6 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Chengzao Sun, Gary Luo, Swetha Neravetla, Soumitra S. Ghosh, Bruce Forood,