Inhibition Profiles of Some Symmetric Sulfamides Derived from Phenethylamines on Human Carbonic Anhydrase I, and II Isoenzymes

New derivatives were synthesised by reaction of amino-containing aromatic sulphonamides with mono-, bi-, and tricyclic anhydrides. These sulphonamides were investigated as human carbonic anhydrases (hCAs, EC 4.2.1.1) I, II, IX, and XII inhibitors. hCA I was inhibited with inhibition constants (Kis) ranging from 49 to >10,000 nM. The physiologically dominant hCA II was significantly inhibited by most of the sulphonamide with the Kis ranging between 2.4 and 4515 nM. hCA IX and hCA XII were inhibited by these sulphonamides in the range of 9.7 to 7766 nM and 14 to 316 nM, respectively. The structure–activity relationships (SAR) are rationalised with the help of molecular docking studies.

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Crystal analysis of aromatic sulfonamide binding to native and (Zn)2 adduct of human carbonic anhydrase I Michigan 1

Inorganica Chimica Acta ◽

10.1016/s0020-1693(02)00959-3 ◽

2002 ◽

Vol 339 ◽

pp. 135-144 ◽

Cited By ~ 6

Author(s):

Marta Ferraroni ◽

Fabrizio Briganti ◽

W.Richard Chegwidden ◽

Claudiu T. Supuran ◽

Andrea Scozzafava

Keyword(s):

Carbonic Anhydrase ◽

Carbonic Anhydrase I ◽

Human Carbonic Anhydrase ◽

Aromatic Sulfonamide

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A simple enzyme-linked immunoassay of human carbonic anhydrase I for the study of developing erythroid cells

Clinica Chimica Acta ◽

10.1016/0009-8981(90)90018-n ◽

1990 ◽

Vol 191 (3) ◽

pp. 169-174 ◽

Cited By ~ 1

Author(s):

Takahito Kondo ◽

Kazuhiro Murakami ◽

Hiroshi Isobe ◽

Naoyuki Taniguchi ◽

Yoshikazu Kawakami

Keyword(s):

Carbonic Anhydrase ◽

Erythroid Cells ◽

Carbonic Anhydrase I ◽

Human Carbonic Anhydrase

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New Histamine-Related Five-Membered N-Heterocycle Derivatives as Carbonic Anhydrase I Activators

Molecules ◽

10.3390/molecules27020545 ◽

2022 ◽

Vol 27 (2) ◽

pp. 545

Author(s):

Niccolò Chiaramonte ◽

Alessio Gabellini ◽

Andrea Angeli ◽

Gianluca Bartolucci ◽

Laura Braconi ◽

...

Keyword(s):

Carbonic Anhydrase ◽

Imidazole Ring ◽

Aliphatic Chain ◽

Amino Group ◽

Carbonic Anhydrase I ◽

Terminal Amino ◽

Human Carbonic Anhydrase ◽

New Compounds ◽

Related Compounds ◽

Micromolar Range

A series of histamine (HST)-related compounds were synthesized and tested for their activating properties on five physiologically relevant human Carbonic Anhydrase (hCA) isoforms (I, II, Va, VII and XIII). The imidazole ring of HST was replaced with different 5-membered heterocycles and the length of the aliphatic chain was varied. For the most interesting compounds some modifications on the terminal amino group were also performed. The most sensitive isoform to activation was hCA I (KA values in the low micromolar range), but surprisingly none of the new compounds displayed activity on hCA II. Some derivatives (1, 3a and 22) displayed an interesting selectivity for activating hCA I over hCA II, Va, VII and XIII.

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