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 Open Access Fibrate-based N-acylsulphonamides targeting carbonic anhydrases: synthesis, biochemical evaluation, and docking studies.(2019-12-01) GIAMPIETRO, L; AMMAZZALORSO, A; CARRADORI, S; ANGELI, A; De, Filippis; FANTACUZZI, M; MACCALLINI, C; Akdemir, ATİLLA; SUPURAN, CT; AMOROSO, R; AKDEMİR, ATİLLAA large library of fibrate-based N-acylsulphonamides was designed, synthesised, and fully characterised in order to propose them as zinc binders for the inhibition of human carbonic anhydrase (hCA) enzymatic activity. Synthesised compounds were tested against four hCAs (I, II, IX, and XII) revealing a promising submicromolar inhibitory activity characterised by an isozyme selectivity pattern. Structural modifications explored within this scaffold are: presence of an aryl ring on the sulphonamide, p-substitution of this aryl ring, benzothiazole or benzophenone as core nuclei, and an n-propyl chain or a geminal dimethyl at Ca carbon. Biological results fitted well with molecular modelling analyses, revealing a putative direct interaction with the zinc ion in the active site of hCA I, II and IX. These findings supported the exploration of less investigated secondary sulphonamides as potential hCA inhibitors.Publication 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.Publication Open Access Computational investigation of the selectivity of salen and tetrahydrosalen compounds towards the tumor-associated hCA XII isozyme.(2015-02-01) Akdemir, ATİLLA; SUPURAN, CT; De, Monte; CARRADORI, S; AKDEMİR, ATİLLAIn previous work, 14 salen and tetrahydrosalen compounds have been synthesized and tested in enzyme inhibition assays against cytosolic human carbonic anhydrase isozymes I and II (hCA I and II) and tumor-associated isozymes IX and XII (hCA IX and XII). These compounds show selectivity against hCA XII over hCA I, II and IX. In this study, molecular modeling and docking studies were applied to understand this preference of the compounds for hCA XII. Most likely, the compounds can displace the zinc-bound water molecule of hCA XII to form a direct interaction with the Zn2+ ion. In the other isozymes, the compounds might not be able to displace the water molecule nor are they expected to interact with the Zn2+ ion.Publication Metadata only Anti-Candida activity and cytotoxicity of a large library of new N-substituted-1,3-thiazolidin-4-one derivatives.(2016-01-01) BIZZARRI, B; MARI, E; ZICARI, A; CARRADORI, S; BOLASCO, A; Akdemir, ATİLLA; De, Monte; SECCI, D; RIVANERA, D; MOLLICA, A; CAPRARA, F; AKDEMİR, ATİLLA