ArticleJournal of enzyme inhibition and medicinal chemistry2020
Synthesis and carbonic anhydrase activating properties of a series of 2-amino-imidazolines structurally related to clonidine
Article in Journal of enzyme inhibition and medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Exploring the Carbonic Anhydrase Activation Properties of 4-arylazo-3,5- diamino-1H-pyrazoles against hCA I, II, IV, and VII isoenzymes.Current topics in medicinal chemistry · 2025Article
- Carbonic Anhydrase Activators for Neurodegeneration: An Overview.Molecules (Basel, Switzerland) · 2022Review
- New Histamine-Related Five-Membered N-Heterocycle Derivatives as Carbonic Anhydrase I Activators.Molecules (Basel, Switzerland) · 2022Article
- Activation of carbonic anhydrases from human brain by amino alcohol oxime ethers: towards human carbonic anhydrase VII selective activators.Journal of enzyme inhibition and medicinal chemistry · 2021Article
- Coumarin carbonic anhydrase inhibitors from natural sources.Journal of enzyme inhibition and medicinal chemistry · 2020Review
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Authors and funding
10 authors.
Funding
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Abstract
The Carbonic Anhydrase (CA, EC 4.2.1.1) activating properties of histamine have been known for a long time. This compound has been extensively modified but only in few instances the imidazole ring has been replaced with other heterocycles. It was envisaged that the imidazoline ring could be a bioisoster of the imidazole moiety. Indeed, we report that clonidine, a 2-aminoimidazoline derivative, was found able to activate several human CA isoforms (hCA I, IV, VA, VII, IX, XII and XIII), with potency in the micromolar range, while it was inactive on hCA II. A series of 2-aminoimidazoline, structurally related to clonidine, was then synthesised and tested on selected hCA isoforms. The compounds were inactive on hCA II while displayed activating properties on hCA I, VA, VII and XIII, with K
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