2. Academic Validation
  3. Synthesis, characterization, inhibition effects, and molecular docking studies as acetylcholinesterase, α-glycosidase, and carbonic anhydrase inhibitors of novel benzenesulfonamides incorporating 1,3,5-triazine structural motifs

Synthesis, characterization, inhibition effects, and molecular docking studies as acetylcholinesterase, α-glycosidase, and carbonic anhydrase inhibitors of novel benzenesulfonamides incorporating 1,3,5-triazine structural motifs

  • Bioorg Chem. 2020 Jul;100:103897. doi: 10.1016/j.bioorg.2020.103897.
Nebih Lolak 1,  Süleyman Akocak 2,  Cüneyt Türkeş 3,  Parham Taslimi 4,  Mesut Işık 5,  Şükrü Beydemir 6,  İlhami Gülçin 7,  Mustafa Durgun 8
Affiliations

Affiliations

  • 1 Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Adıyaman University, Adıyaman 02040, Turkey.
  • 2 Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Adıyaman University, Adıyaman 02040, Turkey. Electronic address: sakocak@adiyaman.edu.tr.
  • 3 Department of Biochemistry, Faculty of Pharmacy, Erzincan Binali Yıldırım University, Erzincan 24100, Turkey.
  • 4 Department of Biotechnology, Faculty of Science, Bartın University, Bartın 74100, Turkey.
  • 5 Department of Pharmacy Services, Vocational School of Health Services, Harran University, Şanlıurfa 63300, Turkey.
  • 6 Department of Biochemistry, Faculty of Pharmacy, Anadolu University, Eskişehir 26470, Turkey.
  • 7 Department of Chemistry, Faculty of Sciences, Atatürk University, Erzurum 25240, Turkey.
  • 8 Department of Chemistry, Faculty of Arts and Sciences, Harran University, Şanlıurfa 63290, Turkey.
PMID: 32413628 DOI: 10.1016/j.bioorg.2020.103897
Abstract

Some metabolic Enzyme inhibitors can be used in the treatment of many diseases. Therefore, synthesis and determination of alternative inhibitors are essential. In this study, the inhibition effect of newly synthesized compounds on Carbonic Anhydrase (cytosolic isoforms, hCA I and hCA II), α-glycosidase (α-GLY), and acetylcholinesterase (AChE) were investigated. The possible binding mechanism of the compounds with a high inhibitory effect on the active site of the Enzyme was demonstrated by molecular docking method. We investigated the inhibition effects of novel synthesized compounds (MZ1-MZ11) on metabolic Enzymes such as α-GLY, AChE, and hCA I and II. The compound MZ6 for AChE, MZ8 for CA I and CA II and MZ7 for α-GLY showed a very active inhibition profile (KIs 51.67 ± 4.76 for hCA I, 40.35 ± 5.74 nM for hCA II, 41.74 ± 8.08 nM for α-GLY and 335.76 ± 46.91 nM for AChE). The novel synthesized compounds (MZ1-MZ11) have a higher Enzyme (α-GLY, AChE, hCA I, and II) inhibitory potential than ACR, TAC, and AZA, respectively. The compounds may have the potential to be used as alternative medicines after further research in the treatment of many diseases such as diabetes, Alzheimer's disease, heart failure, ulcer, and epilepsy.

Keywords

1,3,5-triazine; Anticholinesterase; Carbonic anhydrase; Inhibition; α-glycosidase.

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