ArticleBiophysical journal2020
Isoform-Selective Enzyme Inhibitors by Exploring Pocket Size According to the Lock-and-Key Principle.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Membrane-associated HDAC11: A potential new therapeutic targeting compartment in cancer cells.Biochemistry and biophysics reports · 2026Article
- Di-Journal of medicinal chemistry · 2025Article
- Affinity and Selectivity of Protein-Ligand Recognition: A Minor Chemical Modification Changes Carbonic Anhydrase Binding Profile.Journal of medicinal chemistry · 2025Article
- Article
- PLBD: protein-ligand binding database of thermodynamic and kinetic intrinsic parameters.Database : the journal of biological databases and curation · 2023Article
- Methyl 2-Halo-4-Substituted-5-Sulfamoyl-Benzoates as High Affinity and Selective Inhibitors of Carbonic Anhydrase IX.International journal of molecular sciences · 2021Article
- Switching the Inhibitor-Enzyme Recognition Profile via Chimeric Carbonic Anhydrase XII.ChemistryOpen · 2021Article
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Authors and funding
11 authors.
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Abstract
In the design of high-affinity and enzyme isoform-selective inhibitors, we applied an approach of augmenting the substituents attached to the benzenesulfonamide scaffold in three ways, namely, substitutions at the 3,5- or 2,4,6-positions or expansion of the condensed ring system. The increased size of the substituents determined the spatial limitations of the active sites of the 12 catalytically active human carbonic anhydrase (CA) isoforms until no binding was observed because of the inability of the compounds to fit in the active site. This approach led to the discovery of high-affinity and high-selectivity compounds for the anticancer target CA IX and antiobesity target CA VB. The x-ray crystallographic structures of compounds bound to CA IX showed the positions of the bound compounds, whereas computational modeling confirmed that steric clashes prevent the binding of these compounds to other isoforms and thus avoid undesired side effects. Such an approach, based on the Lock-and-Key principle, could be used for the development of enzyme-specific drug candidate compounds.
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