Tags

Type your tag names separated by a space and hit enter

Novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties.
J Biochem Mol Toxicol. 2018 Sep; 32(9):e22191.JB

Abstract

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.

Authors+Show Affiliations

Department of Chemistry, Faculty of Sciences, Ataturk University, 25240, Erzurum, Turkey.Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029, Baku, Azerbaijan.Department of Biochemistry, Faculty of Veterinary Medicine, Bingol University, 12000, Bingol, Turkey.Health Services Vocational School, Igdır University, 76000, Igdır, Turkey.Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029, Baku, Azerbaijan.Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029, Baku, Azerbaijan.Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives, Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences, 1029, Baku, Azerbaijan.Department of Chemistry, Faculty of Sciences, Ataturk University, 25240, Erzurum, Turkey.Department of Chemistry, Faculty of Sciences, Ataturk University, 25240, Erzurum, Turkey.

Pub Type(s)

Comparative Study
Journal Article

Language

eng

PubMed ID

29992664

Citation

Taslimi, Parham, et al. "Novel Amides of 1,1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, Characterization, Acetylcholinesterase, Butyrylcholinesterase, and Carbonic Anhydrase Inhibitory Properties." Journal of Biochemical and Molecular Toxicology, vol. 32, no. 9, 2018, pp. e22191.
Taslimi P, Osmanova S, Caglayan C, et al. Novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties. J Biochem Mol Toxicol. 2018;32(9):e22191.
Taslimi, P., Osmanova, S., Caglayan, C., Turkan, F., Sardarova, S., Farzaliyev, V., Sujayev, A., Sadeghian, N., & Gulçin, İ. (2018). Novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties. Journal of Biochemical and Molecular Toxicology, 32(9), e22191. https://doi.org/10.1002/jbt.22191
Taslimi P, et al. Novel Amides of 1,1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, Characterization, Acetylcholinesterase, Butyrylcholinesterase, and Carbonic Anhydrase Inhibitory Properties. J Biochem Mol Toxicol. 2018;32(9):e22191. PubMed PMID: 29992664.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties. AU - Taslimi,Parham, AU - Osmanova,Sabiya, AU - Caglayan,Cuneyt, AU - Turkan,Fikret, AU - Sardarova,Sabira, AU - Farzaliyev,Vagif, AU - Sujayev,Afsun, AU - Sadeghian,Nastaran, AU - Gulçin,İlhami, Y1 - 2018/07/10/ PY - 2018/03/25/received PY - 2018/05/07/revised PY - 2018/06/25/accepted PY - 2018/7/12/pubmed PY - 2018/10/30/medline PY - 2018/7/12/entrez KW - acetylcholinesterase KW - carbonic anhydrase KW - enzyme inhibition KW - mercaptoacetic acid KW - p-substituted ketones SP - e22191 EP - e22191 JF - Journal of biochemical and molecular toxicology JO - J. Biochem. Mol. Toxicol. VL - 32 IS - 9 N2 - 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. SN - 1099-0461 UR - https://www.unboundmedicine.com/medline/citation/29992664/Novel_amides_of_11_bis__carboxymethylthio__1_arylethanes:_Synthesis_characterization_acetylcholinesterase_butyrylcholinesterase_and_carbonic_anhydrase_inhibitory_properties_ L2 - https://doi.org/10.1002/jbt.22191 DB - PRIME DP - Unbound Medicine ER -