Novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties
Corresponding Author
Parham Taslimi
Department of Chemistry, Faculty of Sciences, Ataturk University, 25240 Erzurum, Turkey
Correspondence
Parham Taslimi.
Email: [email protected]
Search for more papers by this authorSabiya Osmanova
Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029 Baku, Azerbaijan
Search for more papers by this authorCuneyt Caglayan
Department of Biochemistry, Faculty of Veterinary Medicine, Bingol University, 12000 Bingol, Turkey
Search for more papers by this authorFikret Turkan
Health Services Vocational School, Igdır University, 76000 Igdır, Turkey
Search for more papers by this authorSabira Sardarova
Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029 Baku, Azerbaijan
Search for more papers by this authorVagif Farzaliyev
Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029 Baku, Azerbaijan
Search for more papers by this authorAfsun Sujayev
Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029 Baku, Azerbaijan
Search for more papers by this authorNastaran Sadeghian
Department of Chemistry, Faculty of Sciences, Ataturk University, 25240 Erzurum, Turkey
Search for more papers by this authorİlhami Gulçin
Department of Chemistry, Faculty of Sciences, Ataturk University, 25240 Erzurum, Turkey
Search for more papers by this authorCorresponding Author
Parham Taslimi
Department of Chemistry, Faculty of Sciences, Ataturk University, 25240 Erzurum, Turkey
Correspondence
Parham Taslimi.
Email: [email protected]
Search for more papers by this authorSabiya Osmanova
Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029 Baku, Azerbaijan
Search for more papers by this authorCuneyt Caglayan
Department of Biochemistry, Faculty of Veterinary Medicine, Bingol University, 12000 Bingol, Turkey
Search for more papers by this authorFikret Turkan
Health Services Vocational School, Igdır University, 76000 Igdır, Turkey
Search for more papers by this authorSabira Sardarova
Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029 Baku, Azerbaijan
Search for more papers by this authorVagif Farzaliyev
Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029 Baku, Azerbaijan
Search for more papers by this authorAfsun Sujayev
Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029 Baku, Azerbaijan
Search for more papers by this authorNastaran Sadeghian
Department of Chemistry, Faculty of Sciences, Ataturk University, 25240 Erzurum, Turkey
Search for more papers by this authorİlhami Gulçin
Department of Chemistry, Faculty of Sciences, Ataturk University, 25240 Erzurum, Turkey
Search for more papers by this authorAbstract
The thiolation reaction was carried out in a benzene solution at 80°C and p-substituted ketones and mercaptoacetic acid in a molar ratio (1:4) of in the presence of a catalytic amount of toluene sulfonic acids. The enzyme inhibition activities of the novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes derivatives were investigated. These novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes derivatives showed good inhibitory action against acetylcholinesterase (AChE) butyrylcholinesterase (BChE), and human carbonic anhydrase I and II isoforms (hCA I and II). AChE inhibitors, interacting with the enzyme as their primary target, are applied as relevant drugs and toxins. Many clinically established drugs are carbonic anhydrase inhibitors, and it is highly anticipated that many more will eventually find their way into the market. The novel synthesized compounds inhibited AChE and BChE with Ki values in the range of 0.64–1.47 nM and 9.11–48.12 nM, respectively. On the other hand, hCA I and II were effectively inhibited by these compounds, with Ki values between 63.27–132.34 and of 29.63–127.31 nM, respectively.
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