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Synthesis and Inhibitor Effect Novel Alkoxymethyl Derivatives of Dihetero Cycloalkanes on Carbonic Anhydrase and Acetylcholinesterase.
Farzaliyev, Vagif; Ertürk, Adem; Abbasova, Malahat; Nabiyev, Oruj; Demir, Yeliz; Kiziltas, Hatice; Sujayev, Afsun; Gülçin, Ilhami.
Affiliation
  • Farzaliyev V; Institute of Chemistry of Additives, Ministry of Science and Education of the Republic of Azerbaijan, 1029, Baku, Azerbaijan.
  • Ertürk A; Baku State University, Z. Khalilov Str. 23, AZ-1148, Baku, Azerbaijan.
  • Abbasova M; Ataturk University, Faculty of Science, Department of Chemistry, 25240, Erzurum, Türkiye.
  • Nabiyev O; Institute of Chemistry of Additives, Ministry of Science and Education of the Republic of Azerbaijan, 1029, Baku, Azerbaijan.
  • Demir Y; Institute of Chemistry of Additives, Ministry of Science and Education of the Republic of Azerbaijan, 1029, Baku, Azerbaijan.
  • Kiziltas H; Ardahan University, Nihat Delibalta Göle Vocational High School, Department of Pharmacy Services, 75700, Ardahan, Türkiye.
  • Sujayev A; Van Yüzüncü Yil University, Van Vocational School of Health Services, 65080, Van, Türkiye.
  • Gülçin I; Institute of Chemistry of Additives, Ministry of Science and Education of the Republic of Azerbaijan, 1029, Baku, Azerbaijan.
Chem Biodivers ; 21(6): e202400296, 2024 Jun.
Article in En | MEDLINE | ID: mdl-38575390
ABSTRACT
1,3-Diheterocycloalkanes derivatives are important starting materials in fine organic synthesis. These compounds can be widely used in various fields such as industry, medicine, biotechnology and chemical technology. The paper is focused on synthesis and study of alkoxymethyl derivatives of diheterocycloalkanes (M1-M15) and inhibition effect on carbonic anhydrase and acetylcholinesterase. The structures of compounds were confirmed by 1H and 13C NMR spectroscopy. Also, in this study alkoxymethyl derivatives of diheterocycloalkanes were assessed for their influence on various metabolic enzymes, including acetylcholinesterase (AChE) and human carbonic anhydrase isoenzymes (hCA I and hCA II). The results demonstrated that all these compounds exhibited potent inhibitory effects on all the target enzymes, surpassing the standard inhibitors, as evidenced by their IC50 and Ki values. The Ki values for the compounds concerning AChE, hCA I, and hCA II enzymes were in the ranges of 1.02±0.17-8.38±1.02, 15.30±3.15-58.14±5.17 and 24.05±3.70-312.94±27.24 nM, respectively.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Acetylcholinesterase / Carbonic Anhydrase Inhibitors / Cholinesterase Inhibitors / Cycloparaffins / Carbonic Anhydrase I / Carbonic Anhydrase II Limits: Humans Language: En Journal: Chem Biodivers Journal subject: BIOQUIMICA / QUIMICA Year: 2024 Document type: Article Affiliation country: Azerbaijan Country of publication: Switzerland

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Acetylcholinesterase / Carbonic Anhydrase Inhibitors / Cholinesterase Inhibitors / Cycloparaffins / Carbonic Anhydrase I / Carbonic Anhydrase II Limits: Humans Language: En Journal: Chem Biodivers Journal subject: BIOQUIMICA / QUIMICA Year: 2024 Document type: Article Affiliation country: Azerbaijan Country of publication: Switzerland