Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1372626 | Bioorganic & Medicinal Chemistry Letters | 2009 | 4 Pages |
Abstract
An unnatural amino acid was synthesized to incorporate a quinone methide-generating activity-based probe for protein tyrosine phosphatases (PTPs) and then integrated into a PTP1B-specific substrate. The resulting probe led to preferential labeling of PTP1B in cell lysates in the presence of PTP4A3.
Graphical abstractThe synthesis, peptide incorporation and potential application of an unnatural amino acid containing activity-based probe for protein tyrosine phosphatases are reported.Figure optionsDownload full-size imageDownload as PowerPoint slide
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Kui Shen, Lixin Qi, Mohini Ravula, Krzysztof Klimaszewski,