Preprint Article Version 1 NOT YET PEER-REVIEWED

Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives

Version 1 : Received: 29 September 2016 / Approved: 30 September 2016 / Online: 30 September 2016 (05:38:45 CEST)

A peer-reviewed article of this Preprint also exists.

Genç, H.; Kalin, R.; Köksal, Z.; Sadeghian, N.; Kocyigit, U.M.; Zengin, M.; Gülçin, İ.; Özdemir, H. Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives. Int. J. Mol. Sci. 2016, 17, 1736. Genç, H.; Kalin, R.; Köksal, Z.; Sadeghian, N.; Kocyigit, U.M.; Zengin, M.; Gülçin, İ.; Özdemir, H. Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives. Int. J. Mol. Sci. 2016, 17, 1736.

Journal reference: Int. J. Mol. Sci. 2016, 17, 1736
DOI: 10.3390/ijms17101736

Abstract

β-Lactams are pharmacologically important compounds because of their various biological uses, including antibiotic and so on. β-Lactams were synthesized from benzylidene-inden derivatives and acetoxyacetyl chloride. The inhibitory effect of these compounds was also examined for human carbonic anhydrase I and II (hCA I, and II) and acetylcholinesterase (AChE). The results reveal that β-lactams are inhibitors of hCA I, II and AChE. The Ki values of β-lactams (2a-k) were 0.44-6.29 nM against hCA I, 0.93-8.34 nM against hCA II, and 0.25-1.13 nM against AChE. Our findings indicate that β-lactams (2a-k) inhibit both CA isoenzymes and AChE at low nanomolar concentrations.

Subject Areas

carbonic anhydrase; acetylcholinesterase; β-Lactam; 2-Azetidinone; enzyme inhibition; enzyme purification

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