Over the last decade, research on Carbonic Anhydrases (CAs) has focused on designing and developing novel inhibitors that are specific to certain isoforms to prevent non-specific binding. Many studies have employed computer-assisted drug design to develop selective inhibitors, including non-zinc binding inhibitors. Discrimination of selectivity and bioavailability, along with decreased toxicity optimization, is still lacking. Understanding of isoform-specific structural variation and the lack of corresponding resistance mechanisms, as well as further studies on allosteric modulation and novel binding interactions, are needed. The aim of this review is to investigate the link between chalcone structures and CA inhibition and explore their potential as selective inhibitors. Structural modifications with diverse functional groups are thought to bridge gaps in the discovery of chalcone-based carbonic anhydrase inhibitors. The study emphasizes further exploration of the development of chalcone-based carbonic anhydrase inhibitors.
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Kumar et al. (Mon,) studied this question.
www.synapsesocial.com/papers/69d893a86c1944d70ce04ae1 — DOI: https://doi.org/10.2174/0113894501446010260319103143
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