In Situ Photoregulation of Carbonic Anhydrase Activity Using Azobenzenesulfonamides
Autor: | Brenda P. Medellin, Kanchan Aggarwal, Mandira Banik, Emily L. Que |
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Rok vydání: | 2018 |
Předmět: |
Steric effects
chemistry.chemical_classification Sulfonamides 0303 health sciences biology Photochemistry 030302 biochemistry & molecular biology Active site Biochemistry Small molecule 03 medical and health sciences chemistry.chemical_compound Enzyme Isomerism Azobenzene chemistry Catalytic Domain Carbonic anhydrase biology.protein Biophysics Humans Photodegradation Azo Compounds Cis–trans isomerism Carbonic Anhydrases |
Zdroj: | Biochemistry. 58:48-53 |
ISSN: | 1520-4995 0006-2960 |
Popis: | 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 i... |
Databáze: | OpenAIRE |
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