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@ARTICLE{Rasheed:639284,
      author       = {Rasheed, Saima and Huda, Noo rul and Warsi, Zoha and Tahir,
                      Syeda Sarah and Ahmad, Malik Shoaib and Gul, Sadaf and Arif,
                      Rida and Falke, Sven},
      title        = {{D}rug repurposing: {I}dentification and {X}-ray
                      crystallographic analyses of {US}-{FDA} approved drugs
                      against carbonic anhydrase-{II}},
      journal      = {International journal of biological macromolecules},
      volume       = {305},
      issn         = {0141-8130},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2025-04385},
      pages        = {141057},
      year         = {2025},
      note         = {Waiting for fulltext},
      abstract     = {Of all isoforms, human carbonic anhydrase II (PF00194; EC
                      4.2.1.1), which is mostly found in red cells, kidneys, and
                      the eyes, plays a pivotal role in numerous physiological
                      processes, and its dysregulation has been linked to the wide
                      range of illnesses, such as glaucoma. Finding new inhibitors
                      that target carbonic anhydrase II, therefore has great
                      potential in drug discovery. Using drug repurposing
                      approach, this study focused on the investigation of
                      different drugs as Carbonic anhydrase II inhibitors and
                      their structural studies using X-ray crystallography. For
                      this purpose, 100 different drugs were evaluated for bovine
                      and human carbonic anhydrase II inhibitory activity. Among
                      all, two drugs, i.e. acetohexamide (1) and levosulpiride
                      (54) were found to be active, with IC$_{50}$ = 437.0 ± 0.2
                      and 1128 ± 0.75 μM, respectively. Mechanistic studies
                      suggested that both drugs are competitive inhibitors of the
                      human carbonic anhydrase II enzyme. The X-ray crystal
                      structure analysis revealed that acetohexamide (1) interacts
                      via terminal acetyl group with the active site residues of
                      the carbonic anhydrase II enzyme, and showed strong hydrogen
                      bonding with Zn, His94, His119, and Asn67. The sulfonamide
                      group of levosulpiride was involved in strong hydrogen
                      bonding with Zn, His94, His119, and Thr199. From in vivo
                      studies, we found that carbonic anhydrase activity was
                      significantly inhibited by the intraperitoneal
                      administration of levosulpiride for up to 5 h. Our findings
                      provide comprehensive insights for the optimization of the
                      pharmacological profile of these drugs, and provide avenues
                      for the exploration of different derivatives of these drugs
                      with enhanced efficacy and fewer adverse effects.},
      cin          = {FS-CFEL-1-BMX},
      ddc          = {570},
      cid          = {I:(DE-H253)FS-CFEL-1-BMX-20210408},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1016/j.ijbiomac.2025.141057},
      url          = {https://bib-pubdb1.desy.de/record/639284},
}