Designing and molecular docking analysis of newly acetazolamide derived compounds integrating 4-oxothiazolidine group as possible carbonic anhydrase deactivators
1
Department of Pharmaceutical Chemistry, College of Pharmacy, University of Kufa, Najaf, Iraq, Iraq
2
Department of Pharmaceutical Chemistry, College of Pharmacy, Alzahraa University for Women, Karbala, Iraq, Iraq
Submission date: 2025-07-12
Final revision date: 2025-10-03
Acceptance date: 2026-01-12
Publication date: 2026-01-30
Corresponding author
Shaymaa Abdul Zahra Ayoub
Department of Pharmaceutical Chemistry, College of Pharmacy, University of Kufa, Najaf, Iraq, Iraq
Department of Pharmaceutical Chemistry, College of Pharmacy, University of Kufa, Najaf, Iraq, Iraq
Wiadomości Lekarskie 2026;(1):54-60
KEYWORDS
TOPICS
ABSTRACT
Aim:
Background: Many 4-oxothiazolidine derived compounds have been shown to have various pharmacological properties. Aims: The study aims to create new acetazolamide products that have a thiazolidin-4-one moiety and test how well they stop the carbonic anhydrase XII enzyme (protein data bank code: (4KP5)) and defeat cancer in silico.
Material and methods:
Materials and methods: We will make four acetazolamide derivatives that have a thiazolidin-4-one group. Acetazolamide will be the starting material. We used the Molecular Operating Environment program 2015.10 to figure out the molecular docking studies. Root Mean Square Deviation (RMSD) and Standard Score (S. score) were used to describe docking how well docked ligands stuck to the target protein carbonic anhydrase XII.
Results:
Results: The process of docking showed that the four test ligands (IIIa, IIIb, IIIc, and IIId) bound to the target protein carbonic anhydrase XII more strongly than the reference ligand, which is an acetazolamide.
Conclusions:
Conclusion: Of the four chemicals, IIIa had the maximum affinity for binding and a S. score of -7.39. The results propose that the acetazolamide compounds that were designed, especially IIIa, could be carbonic anhydrase inhibitors and anti-cancer drugs that work on the carbonic anhydrase XII enzyme.
Background: Many 4-oxothiazolidine derived compounds have been shown to have various pharmacological properties. Aims: The study aims to create new acetazolamide products that have a thiazolidin-4-one moiety and test how well they stop the carbonic anhydrase XII enzyme (protein data bank code: (4KP5)) and defeat cancer in silico.
Material and methods:
Materials and methods: We will make four acetazolamide derivatives that have a thiazolidin-4-one group. Acetazolamide will be the starting material. We used the Molecular Operating Environment program 2015.10 to figure out the molecular docking studies. Root Mean Square Deviation (RMSD) and Standard Score (S. score) were used to describe docking how well docked ligands stuck to the target protein carbonic anhydrase XII.
Results:
Results: The process of docking showed that the four test ligands (IIIa, IIIb, IIIc, and IIId) bound to the target protein carbonic anhydrase XII more strongly than the reference ligand, which is an acetazolamide.
Conclusions:
Conclusion: Of the four chemicals, IIIa had the maximum affinity for binding and a S. score of -7.39. The results propose that the acetazolamide compounds that were designed, especially IIIa, could be carbonic anhydrase inhibitors and anti-cancer drugs that work on the carbonic anhydrase XII enzyme.
| eISSN: | 2719-342X |
| ISSN: | 0043-5147 |
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