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<p>In order to find new inhibitors for human carbonic anhydrase I and II, this research uses both in vitro and in silico approaches. Schiff bases were synthesized by adding a sulphonamide group to pyrazole derivative. Using standard spectroscopic methods, the synthesised compounds <b>(7–14)</b> were structurally characterised. The AutoDock Vina 1.2.3 program was then used to perform molecular docking investigations for these compounds against Human carbonic anhydrase I (PDB ID: 1azm) and Human carbonic anhydrase II (PDB ID: 3hs4). All the compounds had greater binding affinities than the typical acetazolamide, according to the docking studies. Compounds <b>7</b> and <b>9</b> were chosen for molecular dynamic modelling because they had the greatest binding affinities for the hCA I and hCA II proteins, respectively. The dynamic behaviour, stability of the protein–ligand complex, and binding affinity of compounds <b>7</b> and <b>9</b> were evaluated using molecular dynamic (MD) simulations. These simulations indicated that compounds <b>7</b> and <b>9</b> exhibit stable interactions with hCA I and hCA II, respectively. Among the synthesized derivatives, compounds <b>7</b> and <b>9</b> showed comparatively better inhibitory activity, although their potency remained lower than the reference inhibitor acetazolamide. Overall, the results suggest that pyrazole-based Schiff base derivatives possess moderate inhibitory activity against human carbonic anhydrase I and II and may serve as a useful scaffold for further optimization.</p>

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In vitro and in silico evaluation of a new schiff base: carbonic anhydrase I and II enzyme inhibition, molecular docking, and dynamic behaviour

  • 期刊论文

  • 发表日期：

    2026年4月22日

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  • Viswaskumar Panchal,
  • Zakirhusen Gadhawala,
  • Arun Malaviya,
  • Simone Giovannuzzi,
  • Claudiu T. Supuran

摘要

In order to find new inhibitors for human carbonic anhydrase I and II, this research uses both in vitro and in silico approaches. Schiff bases were synthesized by adding a sulphonamide group to pyrazole derivative. Using standard spectroscopic methods, the synthesised compounds (7–14) were structurally characterised. The AutoDock Vina 1.2.3 program was then used to perform molecular docking investigations for these compounds against Human carbonic anhydrase I (PDB ID: 1azm) and Human carbonic anhydrase II (PDB ID: 3hs4). All the compounds had greater binding affinities than the typical acetazolamide, according to the docking studies. Compounds 7 and 9 were chosen for molecular dynamic modelling because they had the greatest binding affinities for the hCA I and hCA II proteins, respectively. The dynamic behaviour, stability of the protein–ligand complex, and binding affinity of compounds 7 and 9 were evaluated using molecular dynamic (MD) simulations. These simulations indicated that compounds 7 and 9 exhibit stable interactions with hCA I and hCA II, respectively. Among the synthesized derivatives, compounds 7 and 9 showed comparatively better inhibitory activity, although their potency remained lower than the reference inhibitor acetazolamide. Overall, the results suggest that pyrazole-based Schiff base derivatives possess moderate inhibitory activity against human carbonic anhydrase I and II and may serve as a useful scaffold for further optimization.