Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1364602 | Bioorganic & Medicinal Chemistry Letters | 2008 | 4 Pages |
Abstract
The peptide ligase subtiligase, derived from subtilisin, has been employed in the identification of protein N-termini in complex mixtures. Here, the peptide ester substrates for the ligation reaction were optimized with respect to solubility, resulting in greater incorporation of the N-terminal tags. Additionally, the quantitation of the incorporated tags was explored, and a ‘click’ chemistry-based derivatization provided the ability to quantitate the tag to low nanomolar concentrations by sandwich ELISA. These new tags should expand the utility of subtiligase for the proteomic study of N-termini.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Hikari A.I. Yoshihara, Sami Mahrus, James A. Wells,