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Fibrate-based N-acylsulphonamides targeting carbonic anhydrases: synthesis, biochemical evaluation, and docking studies.

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Date
2019-12-01
Authors
GIAMPIETRO, L
AMMAZZALORSO, A
CARRADORI, S
ANGELI, A
De, Filippis
FANTACUZZI, M
MACCALLINI, C
Akdemir, ATİLLA
SUPURAN, CT
AMOROSO, R
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Abstract
A large library of fibrate-based N-acylsulphonamides was designed, synthesised, and fully characterised in order to propose them as zinc binders for the inhibition of human carbonic anhydrase (hCA) enzymatic activity. Synthesised compounds were tested against four hCAs (I, II, IX, and XII) revealing a promising submicromolar inhibitory activity characterised by an isozyme selectivity pattern. Structural modifications explored within this scaffold are: presence of an aryl ring on the sulphonamide, p-substitution of this aryl ring, benzothiazole or benzophenone as core nuclei, and an n-propyl chain or a geminal dimethyl at Ca carbon. Biological results fitted well with molecular modelling analyses, revealing a putative direct interaction with the zinc ion in the active site of hCA I, II and IX. These findings supported the exploration of less investigated secondary sulphonamides as potential hCA inhibitors.
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N-acylsulphonamides, PPAR antagonist, Benzophenone, Benzothiazole, Carbonic anhydrase, Fibrate derivatives
Citation
AMMAZZALORSO A., CARRADORI S., ANGELI A., Akdemir A., De F., FANTACUZZI M., GIAMPIETRO L., MACCALLINI C., AMOROSO R., SUPURAN C., -Fibrate-based N-acylsulphonamides targeting carbonic anhydrases: synthesis, biochemical evaluation, and docking studies.-, Journal of enzyme inhibition and medicinal chemistry, cilt.34, ss.1051-1061, 2019
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