Carbonic Anhydrase Interaction with Lipothioarsenites
Author Information
Author(s): Despina Timotheatou, Pana,viotis V. Ioannou, Andrea Scozzafava, Fabrizio Briganti, Claudiu T. Supuran
Primary Institution: University of Patras, Department of Chemistry, Patras, Greece
Hypothesis
The study investigates the interaction of carbonic anhydrase isozymes I and II with a series of As(III) derivatives to identify potential inhibitors.
Conclusion
Lipothioarsenites with at least one COOH group can inhibit carbonic anhydrase isozymes I and II by binding to the Co(II) ion in the enzyme.
Supporting Evidence
- The study found that lipothioarsenites are effective inhibitors of carbonic anhydrase isozymes I and II.
- Active compounds were identified that contain carboxyl groups, while those with aromatic groups were mostly inactive.
- The binding of inhibitors to the enzyme was confirmed through changes in electronic spectra.
Takeaway
Some new compounds can stop a specific enzyme in our body that helps with many processes, and they work best when they have a certain group attached to them.
Methodology
The interaction was investigated kinetically and spectrophotometrically using native and Co(II)-substituted enzymes.
Limitations
The inactive compounds were found for certain substitution patterns, and the stability of the enzyme-inhibitor adducts was limited.
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