Protein tyrosine phosphatases (PTPs) are key signaling enzymes involved in both pathological and physiological processes and have been implicated in numerous human diseases including bacterial infections, autoimmune disorders, diabetes, and cancer. In order to advance our understanding of these important enzymes with the aim of realizing their potential as therapeutic targets, the chemical toolkit available for studying the PTPs must be expanded as many existing probes are incompatible with cellular applications. In this work, a resorufin-based PTP substrate, pRes, has been synthesized. pRes has red-shifted emission and excitation profiles as compared to existing substrates and has been used as a fluorogenic substrate to monitor human PTP activity both <i>in vitro</i> and in living cells and validated for use in high throughput screening. In addition, pRes was used for colorimetric visual detection of the pathogenic bacteria <i>Staphylococcus aureus</i>. Finally, a fluorinated version of pRes was synthesized and utilized for monitoring the activity of tyrosine phosphatases active at acidic pH.

Developing dual colorimetric and fluorogenic probes for visualizing tyrosine phosphatase activity and high throughput screening

253rd National Meeting (2017)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.