A series of sulfamide fragments has been synthesised and investigated for human carbonic anhydrase inhibition. One of the fragments showing greater selectivity for cancer-related isoforms hCA IX and XII was co-crystalized with hCA II showing significant potential for fragment periphery evolution via fragment growth and linking. These opportunities will be identified in the future via the screening of this fragment structure for co-operative carbonic anhydrase binding with other structurally diverse fragments.

Original languageEnglish
Pages (from-to)857-865
Number of pages9
JournalJournal of Enzyme Inhibition and Medicinal Chemistry
Volume37
Issue number1
DOIs
StatePublished - 16 Mar 2022

    Scopus subject areas

  • Drug Discovery
  • Pharmacology

    Research areas

  • Carbonic anhydrase, co-operative fragment screening, solubility, sulfamides, zinc-binding groups, Humans, Structure-Activity Relationship, Drug Discovery, Dose-Response Relationship, Drug, Carbonic Anhydrase Inhibitors/chemical synthesis, Carbonic Anhydrases/metabolism, Molecular Structure, Sulfonamides/chemical synthesis, Isoenzymes/antagonists & inhibitors, DESIGN, SULFONAMIDES, OF-THE-ART, FAMOTIDINE, ISOZYME-II

ID: 94010611