Person: AKDEMİR, ATİLLA
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Publication Metadata only A novel library of saccharin and acesulfame derivatives as potent and selective inhibitors of carbonic anhydrase IX and XII isoforms.(2016-03-01) CERUSO, M; SECCI, D; De, Monte; MOLLICA, A; SOBOLEV, AP; Akdemir, ATİLLA; SUPURAN, CT; GUGLIELMI, P; De, Cosmi; CODISPOTI, R; CARRADORI, S; AKDEMİR, ATİLLAPublication Metadata only Exploring new Probenecid-based carbonic anhydrase inhibitors: Synthesis, biological evaluation and docking studies.(2015-09-01) MOLLICA, A; COSTANTE, R; Akdemir, ATİLLA; CARRADORI, S; STEFANUCCI, A; MACEDONIO, G; CERUSO, M; SUPURAN, CT; AKDEMİR, ATİLLAPublication Metadata only New amide derivatives of Probenecid as selective inhibitors of carbonic anhydrase IX and XII: biological evaluation and molecular modelling studies.(2015-07-01) De, Monte; SABIA, R; MOLLICA, A; CERUSO, M; CARRADORI, S; D'ASCENZIO, M; CHIMENTI, P; Akdemir, ATİLLA; SUPURAN, CT; AKDEMİR, ATİLLAPublication Metadata only Selective inhibition of human carbonic anhydrases by novel amide derivatives of probenecid: synthesis, biological evaluation and molecular modelling studies.(2014-08-01) D'ASCENZIO, M; CARRADORI, S; SECCI, D; VULLO, D; CERUSO, M; Akdemir, ATİLLA; SUPURAN, CT; AKDEMİR, ATİLLAPublication Open Access Open saccharin-based secondary sulfonamides as potent and selective inhibitors of cancer-related carbonic anhydrase IX and XII isoforms.(2017-12-01) D'ASCENZIO, M; GUGLIELMI, P; CARRADORI, S; SECCI, D; FLORIO, R; MOLLICA, A; CERUSO, M; Akdemir, ATİLLA; SOBOLEV, AP; SUPURAN, CT; AKDEMİR, ATİLLAA large number of novel secondary sulfonamides based on the open saccharin scaffold were synthesized and evaluated as selective inhibitors of four different isoforms of human carbonic anhydrase (hCA I, II, IX and XII, EC 4.2.1.1). They were obtained by reductive ring opening of the newly synthesized N-alkylated saccharin derivatives and were shown to be inactive against the two cytosolic off-target hCA I and II (Kis > 10 µM). Interestingly, these compounds inhibited hCA IX in the low nanomolar range with Kis ranging between 20 and 298 nM and were extremely potent inhibitors of hCA XII isoenzyme (Kis ranging between 4.3 and 432 nM). Since hCA IX and XII are the cancer-related isoforms recently validated as drug targets, these results represent an important goal in the development of new anticancer candidates. Finally, a computational approach has been performed to better correlate the biological data to the binding mode of these inhibitors.