| Literature DB >> 26264840 |
Adriano Mollica1, Roberto Costante2, Atilla Akdemir3, Simone Carradori2, Azzurra Stefanucci4, Giorgia Macedonio2, Mariangela Ceruso5, Claudiu T Supuran6.
Abstract
Novel Probenecid-based amide derivatives, incorporating different natural amino acids, were synthesized and assayed to test their effect on the human carbonic anhydrase (hCA, EC 4.2.1.1) transmembrane isoforms hCA IX and XII over the ubiquitous isoforms hCA I and II. Most of them presented a complete loss of hCA II inhibition (K(i)s > 10,000 nM) and strong inhibitory activity against hCA IX and XII in the nanomolar range with respect to the parent compound. A residual activity against hCA I was observed for some of them. These biological results have been explained by docking studies within the active sites of the four studied human carbonic anhydrases (with or without the zinc-bound water) and helped us to better comprehend the rationale behind the design of tertiary sulfonamide compounds as potent but atypical inhibitors of specific isoforms of human carbonic anhydrase.Entities:
Keywords: Molecular modeling; Probenecid; Selective carbonic anhydrase IX inhibitors; Selective carbonic anhydrase XII inhibitors; Tertiary sulfonamides
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Year: 2015 PMID: 26264840 DOI: 10.1016/j.bmc.2015.07.066
Source DB: PubMed Journal: Bioorg Med Chem ISSN: 0968-0896 Impact factor: 3.641