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Redox-Based Probes for Protein Tyrosine Phosphatases

Authors


  • We acknowledge funding from the Camille and Henry Dreyfus Teacher–Scholar Awards Program (to K.S.C.) and the American Heart Association Scientist Development Award (award number 0835419N to K.S.C.). We thank Prof. M. Saper for providing the YopH expression plasmid and for helpful discussion, Jesse Song for providing technical assistance, and Prof. A. Barrios for helpful discussion.

Abstract

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Three in one: The design strategy for redox-based probes (RBPs) that detect the reversible oxidation of protein tyrosine phosphatases (PTPs) includes a “warhead” that forms a covalent adduct with the oxidized active site cysteine of PTPs, a synthetic module that directs binding to the PTP active site, and a chemical reporter tag used for the identification, purification, or direct visualization of the probe-labeled proteins (see picture).

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