| Literature DB >> 31784185 |
Alessio Nocentini1, Davide Moi2, Alessandro Deplano3, Sameh M Osman4, Zeid A AlOthman4, Gianfranco Balboni2, Claudiu T Supuran1, Valentina Onnis5.
Abstract
We report here a thorough structure-activity relationship (SAR) with piperazinylureido sulfamates as inhibitors of human (h) carbonic anhydrase (CA, EC 4.2.1.1). A SAR investigation over the structure of reported anti-cancer zinc-binder CAIs such as SLC-0111 and S4 was carried out by including the urea outer nitrogen atom into a substituted piperazine ring reducing the linker flexibility. The derivatives were assessed for the inhibition of CA I, II and IV (off-target isoforms) and the tumor-associated CA IX (anticancer drug target). CA I and IV were not effectively inhibited, whereas many low nanomolar inhibitors were evidenced against CA II (KIs in the range of 1.0-705.5 nM), and IX (KIs in the range of 0.91-155.9 nM). Interestingly, a subset of CA II/IX selective inhibitors was detected which might represent interesting lead for the development of new anticancer strategies.Entities:
Keywords: Antitumor; Bioisoster; Inhibitor; Metalloenzyme; Selectivity
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Year: 2019 PMID: 31784185 DOI: 10.1016/j.ejmech.2019.111896
Source DB: PubMed Journal: Eur J Med Chem ISSN: 0223-5234 Impact factor: 6.514