Diversely substituted sulfamides for fragment-based drug discovery of carbonic anhydrase inhibitors

Diversely substituted sulfamides for fragment-based drug discovery of carbonic anhydrase inhibitors: synthesis and inhibitory profile

Research output: Contribution to journal › Article › peer-review

DOI

https://doi.org/10.1080/14756366.2022.2051023
Final published version

Tatiana Sharonova
Petr Zhmurov
Stanislav Kalinin
Alessio Nocentini
Andrea Angeli
Marta Ferraroni
Mikhail Korsakov
Claudiu T. Supuran
Mikhail Krasavin

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 language	English
Pages (from-to)	857-865
Number of pages	9
Journal	Journal of Enzyme Inhibition and Medicinal Chemistry
Volume	37
Issue number	1
DOIs	https://doi.org/10.1080/14756366.2022.2051023
State	Published - 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