Tayfun Arslan

Synthesis and Biological Evaluation of Novel Bischalcone Derivatives as Carbonic Anhydrase Inhibitors.

Design and synthesis of a new type of bischalcones as an alternative to natural and synthetic bischalcones are reported for the first time. Key steps involved the solvent‐free Claisen–Schmidt condensation of chalcones, and the successful first application of the diazotization–diazocoupling reaction in the synthesis of CNNC‐linked bischalcones by simple structural modification of p‐aminoacetophenone. The structures of all compounds were confirmed by means of FT‐IR, 1H and 13C NMR, ESI/MS, and elemental analysis. In addition, the newly synthesized compounds were screened for carbonic anhydrase inhibition activities. Almost all bischalcones exhibited moderate‐to‐good inhibitory activities.

Synthesis and carbonic anhydrase inhibitory properties of novel chalcone substituted benzenesulfonamides

Carbonic anhydrases (CAs, EC 4.2.1.1) are crucial metalloenzymes involved in many bioprocesses, through catalysis of the reversible hydration/dehydration process of CO2/HCO3-. The inhibition of human CA isoforms I and II with a new series of sulfonamide derivatives incorporating substituted chalcone moieties were studied in this study. All these newly synthesized sulfonamides demonstrated important inhibitory profiles to these CA isoforms with KIs in the range of 9.88 to 55.43nM, making these compounds interesting leads, with potential applications in medicinal chemistry.

The synthesis of axially disubstituted silicon phthalocyanines, their quaternized derivatives and first inhibitory effect on human cytosolic carbonic anhydrase isozymes hCA I and II

In this study a novel silicon(IV) phthalocyanine bearing [(2E)-3-[4-(dimethylamino)phenyl]-1-(4-phenoxy)prop-2-en-1-one] group and its quaternized derivative at their axial positions were synthesized for the first time. Axially disubstituted silicon(IV) phthalocyanines were also characterized by various spectroscopic techniques. The inhibition of two human cytosolic carbonic anhydrase (hCA, EC 4.2.1.1) isozymes I and II, with axially disubstituted silicon phthalocyanines and their quaternized derivatives were investigated by using the esterase assay, with 4-nitrophenyl acetate as substrate. Silicon phthalocyanines ZM-1-Si, ZM-5-Si, ZT-Si and their quaternized derivatives ZM-1-SiQ, ZM-5-SiQ, ZT-SiQ showed IC50 values in the range of 0.0178–0.1653 μM for hCA I and of 0.0172–0.1212 μM against hCA II, respectively. This study is the first example of carbonic anhydrase enzyme inhibition of phthalocyanines.

Corrigendum to “Synthesis and carbonic anhydrase inhibitory properties of novel chalcone substituted benzenesulfonamides” [Bioorg. Med. Chem. Lett. 26 (2016) 5867–5870]

a Technical Sciences Vocational School, Giresun University, 28049 Giresun, Turkey Ağrı _ Ibrahim Çeçen University, Department of Pharmaceutical Technology, 04100 Ağrı, Turkey Ağrı _ Ibrahim Çeçen University, Science and Art Faculty, Chemistry Department, 04100 Ağrı, Turkey Universitá degli Studi di Firenze, Dipartimento Neurofarba, Sezione di Scienze, Polo Scientifico, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Florence, Italy