2. Academic Validation
  3. In Situ Photoregulation of Carbonic Anhydrase Activity Using Azobenzenesulfonamides

In Situ Photoregulation of Carbonic Anhydrase Activity Using Azobenzenesulfonamides

  • Biochemistry. 2019 Jan 8;58(1):48-53. doi: 10.1021/acs.biochem.8b00947.
Kanchan Aggarwal 1,  Mandira Banik 1,  Brenda Medellin 2,  Emily L Que 1
Affiliations

Affiliations

  • 1 Department of Chemistry , The University of Texas at Austin , 105 East 24th Street, Stop A5300 , Austin , Texas 78712 , United States.
  • 2 Department of Molecular Biosciences and Institute for Cellular and Molecular Biology , The University of Texas at Austin , 100 East 24th Street, Stop A5000 , Austin , Texas 78712 , United States.
PMID: 30358990 DOI: 10.1021/acs.biochem.8b00947
Abstract

We report two small molecule azobenzenesulfonamide probes, CAP1 and CAP2, capable of photomodulating the activity of Carbonic Anhydrase (CA) on demand. In the trans form, CAP azobenzene probes adopt a linear shape, making them suitable for occupying the CA active site and interacting with Zn2+, thereby inhibiting Enzyme activity. Following irradiation with either 365 or 410 nm light, the CAP probes isomerize to their cis form. Because of the change in steric profile, the probe exits the active site, and the activity of the Enzyme is restored. The cis isomer can revert back to the trans isomer through thermal relaxation or via photoirradiation with 460 nm light and thereby inhibit protein activity again. This process can be repeated multiple times without any photodegradation and thus can be used to inhibit or activate the protein reversibly. Importantly, we demonstrate our ability to apply CAP azobenzene probes to regulate CA activity both in an isolated protein solution and in live cells, where the two isomers of CAP1 differentially regulate the intracellular cytosolic pH.

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