280563-35-1Relevant academic research and scientific papers
Carbonic anhydrase inhibitors: Synthesis of sulfonamides incorporating dtpa tails and of their zinc complexes with powerful topical antiglaucoma properties
Scozzafava, Andrea,Menabuoni, Luca,Mincione, Francesco,Mincione, Giovanna,Supuran, Claudiu T
, p. 575 - 582 (2001)
Reaction of diethylenetriamino pentaacetic acid (dtpa) dianhydride with aromatic/heterocyclic sulfonamides possessing a free amino/imino/hydrazino/hydroxy group afforded bis-sulfonamides containing metal-complexing, polyamino-polycarboxylic acid moieties in their molecule. The corresponding mono-sulfonamide derivatives of dtpa were also obtained by an alternative method, from the free acid. Zn(II) complexes of these new sulfonamides were then prepared. Many of these derivatives showed nanomolar affinity towards isozymes I, II and IV of carbonic anhydrase (CA). Some of the best inhibitors were applied as 2% water solutions/suspensions into the eye of normotensive or glaucomatous albino rabbits, when strong and long-lasting intraocular pressure (IOP) lowering was observed.
Sulfonamide-functionalized gadolinium DTPA complexes as possible contrast agents for MRI: A relaxometric investigation
Anelli, Pier Lucio,Bertini, Ivano,Fragai, Marco,Lattuada, Luciano,Luchinat, Claudio,Parigi, Giacomo
, p. 625 - 630 (2007/10/03)
A novel Gd-DTPA derivative with a built-in sulfonamide (SA) was synthesized as a contrast agent for MRI. The complex was designed to selectively target the enzyme carbonic anhydrase. It is shown that the longitudinal relaxation rates of aqueous solutions of Gd-DTPA-SA in the presence of carbonic anhydrase increase significantly. The binding constant is determined to be 15,000 ± 5,000 M-1. This value ensures substantial formation of the carbonic anhydrase adduct at imaging concentrations of Gd- DTPA-SA. The complex interacts with erythrocytes, presumably due to a high affinity for the carbonic anhydrase present on the outer surface of the latter. This takes place even though the enzyme has a low abundance and is easily saturated by small amounts of Gd-DTPA-SA. The interaction of Gd-DTPA- SA with serum proteins is negligibly small. Therefore, the complex could potentially be tested as a selective contrast agent for compartments outside the blood pool.
