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Updated: Jul 6, 2026

Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization
Published on: March 16, 2020
Carbonic anhydrase activation and the drug design
Claudia Temperini1, Andrea Scozzafava, Claudiu T Supuran
1Università degli Studi di Firenze, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, I-50019 Sesto Fiorentino (Firenze), Italy. claudia.temperini@unifi.it
Abstract:
The activation mechanism of Carbonic Anhydrase was recently explained using kinetic, spectroscopic and X-ray techniques. It has been demonstrated that the activators molecules (CAAs) bind at the entrance of the enzyme active-site facilitating the rate-determining step of CA catalytic cycle. Drug design studies have been performed in order to obtain strong CAAs belonging to several chemical classes: amino acids, azoles, amine and their derivatives, etc. Structure-activity correlations of different activators are discussed for the most studied Carbonic Anhydrase isozymes: isoform I and II. The physiological relevance of CA activation and the possible application of CAAs in Alzheimer's disease and for other memory therapies are also treated.
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