Your browser doesn't support javascript.
loading
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.
Afiliación
  • 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 en 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.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Acetilcolinesterasa / Inhibidores de Anhidrasa Carbónica / Inhibidores de la Colinesterasa / Cicloparafinas / Anhidrasa Carbónica I / Anhidrasa Carbónica II Límite: Humans Idioma: En Revista: Chem Biodivers Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Azerbaiyán

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Acetilcolinesterasa / Inhibidores de Anhidrasa Carbónica / Inhibidores de la Colinesterasa / Cicloparafinas / Anhidrasa Carbónica I / Anhidrasa Carbónica II Límite: Humans Idioma: En Revista: Chem Biodivers Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Azerbaiyán