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AKDEMİR, ATİLLA

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ATİLLA
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AKDEMİR
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2013 - 20197
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Now showing 1 - 7 of 7
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    PublicationOpen Access
    The extremo-α-carbonic anhydrase (CA) from Sulfurihydrogenibium azorense, the fastest CA known, is highly activated by amino acids and amines.
    (2013-02-15) CARGINALE, V; CAPASSO, C; SUPURAN, CT; VULLO, D; De, Luca; SCOZZAFAVA, A; ROSSI, M; Akdemir, ATİLLA; AKDEMİR, ATİLLA
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    PublicationOpen Access
    Novel thiazolidinone-containing compounds, without the well-known sulphonamide zinc-binding group acting as human carbonic anhydrase IX inhibitors.
    (2018-12-01) DEMIR, K; Akdemir, ATİLLA; ANGELI, A; GÜZEL-AKDEMIR, Ö; SUPURAN, CT; AKDEMİR, ATİLLA
    A small collection of 26 structurally novel thiazolidinone-containing compounds, without the well-known sulphonamide zinc-binding group, were synthesised and tested in enzyme inhibition assays against the tumour-associated hCA IX enzyme. Inhibition constants in the lower micromolar region (KI < 25 lM) have been measured for 17 of the 26 compounds. Even though the KI values are relatively weak, the fact that they do not contain a sulphonamide moiety suggests that these compounds do not interact with the active site zinc ion. Therefore, docking studies and molecular dynamics simulations have been performed to suggest binding poses for these structurally novel inhibitors.
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    PublicationOpen 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, ATİLLA
    A 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.
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    PublicationOpen Access
    Novel 2-indolinones containing a sulfonamide moiety as selective inhibitors of candida β-carbonic anhydrase enzyme.
    (2019-12-01) Akdemir, ATİLLA; ANGELI, A; GÖKTAŞ, F; Eraslan, Elma; KARALı, N; SUPURAN, CT; Inhibition of the b-carbonic anhydrase (CA, EC 4.2.1.1) from pathogenic Candida glabrata (CgNce103) by 1H-indole-2,3-dione 3-[N-(4-sulfamoylphenyl)thiosemicarbazones] 4a–m was investigated. All the compounds were found to be potent inhibitors of CgNce103, with inhibition constants in the range of 6.4- 63.9 nM. The 5,7-dichloro substituted derivative 4l showed the most effective inhibition (KI of 6.4 nM) as well as the highest selectivity for inhibiting CgNce103 over the cytosolic human (h) isoforms hCA I and II. A possible binding interaction of compound 4l within the active site of CgNce103 has been proposed based on docking studies.; AKDEMİR, ATİLLA
    Inhibition of the b-carbonic anhydrase (CA, EC 4.2.1.1) from pathogenic Candida glabrata (CgNce103) by 1H-indole-2,3-dione 3-[N-(4-sulfamoylphenyl)thiosemicarbazones] 4a–m was investigated. All the compounds were found to be potent inhibitors of CgNce103, with inhibition constants in the range of 6.4- 63.9 nM. The 5,7-dichloro substituted derivative 4l showed the most effective inhibition (KI of 6.4 nM) as well as the highest selectivity for inhibiting CgNce103 over the cytosolic human (h) isoforms hCA I and II. A possible binding interaction of compound 4l within the active site of CgNce103 has been proposed based on docking studies.
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    PublicationOpen 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, ATİLLA
    A 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.
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    PublicationOpen 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, ATİLLA
    In 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.
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    PublicationOpen Access
    Discovery of novel isatin-based sulfonamides with potent and selective inhibition of the tumor-associated carbonic anhydrase isoforms IX and XII.
    (2015-06-21) GÜZEL-AKDEMIR, Ö; Akdemir, ATİLLA; KARALı, N; SUPURAN, CT; AKDEMİR, ATİLLA
    A series of 2/3/4-[(2-oxo-1,2-dihydro-3H-indol-3-ylidene)amino]benzenesulfonamides, obtained from substituted isatins and 2-, 3- or 4-aminobenzenesulfonamide, showed low nanomolar inhibitory activity against the tumor associated carbonic anhydrase (CA, EC 4.2.1.1) isoforms IX and XII – recently validated antitumor drug targets, being much less effective as inhibitors of the off-target cytosolic isoforms CA I and II.