Disease relevance of NSC252

• Inhibitors of the C(2)-symmetric HIV-1 protease: nonsymmetric binding of a symmetric cyclic sulfamide with ketoxime groups in the P2/P2' side chains [1].
• Heparinoids with different sulfamide contents indicated that the anticoagulant activity (35.3-41.3 units/mg) is independent of the sulfamide content, while an increase in sulfamide content lowered the toxicity [2].
• Generalized cutaneous depigmentation following sulfamide-induced drug eruption [3].

High impact information on NSC252

• In other cases, the sulfamide moiety is important for inducing desired physico-chemical properties to the drug-like compounds incorporating it, such as enhanced water solubility, better bioavailability, etc., because of the intrinsic properties of this highly polarized moiety when attached to an organic scaffold [4].
• Long chain saturated and unsaturated alkyl sulfamide and propyl sulfamide derivatives, analogs of oleoylethanolamide, have been synthesized and evaluated in vivo and in vitro as peroxisome proliferator activated receptor alpha (PPARalpha) activators [5].
• These results indicate that the sulfamide moiety is not particularly suitable for obtaining potent carbonic anhydrase inhibition [6].
• Comparison of sulfamate and sulfamide groups for the inhibition of carbonic anhydrase-II by using topiramate as a structural platform [6].
• Sulfamide-based inhibitors for carboxypeptidase A. Novel type transition state analogue inhibitors for zinc proteases [7].

Chemical compound and disease context of NSC252

• The toxicity to mice and/or houseflies decreases in the following order: TETS much greater than the heterotetracyclic compound hexamethylenetrisulfohexamine (HEXS) and two TETS analogues in which one sulfamide group is replaced with o-phenylenediamine or 1,1-dimethyl-1,2-diaminoethane much greater than seven other hetero(homo)adamantanes [8].
• To identify structural features associated with a certain resistance profile, the inhibitory properties of a series of symmetric and asymmetric cyclic sulfamide, cyclic urea and linear transition-state analogue inhibitors of HIV-1 protease were investigated using wild-type and mutant enzyme [9].

Anatomical context of NSC252

• Protons may effectively be transported across lipid membranes with a maximum at a pH close to the pKa of the sulfamide (pKa of glibenclamide = 5.4) [10].

Associations of NSC252 with other chemical compounds

• Topiramate (1) and its sulfamide analogue 4, and 4,5-cyclic sulfate 6 and its sulfamide analogue 5, were compared for inhibition of human CA-II [6].
• Carbonic anhydrase inhibitors: inhibition of isozymes I, II and IV by sulfamide and sulfamic acid derivatives [11].
• The identification, design, and synthesis of a series of novel sulfamide- and urea-based small-molecule antagonists of the protein-protein interaction IL-2/IL-2Ralpha are described [12].
• A series of N-cyanosulfonamides has been prepared by reaction of alkyl-, arylalkyl- and arylsulfonyl halides or sulfonic acid anhydrides with cyanamide, or by reaction of cyanogen bromide with sulfamide/sulfamic acid [13].

Gene context of NSC252

• A series of sugar sulfamate/sulfamide derivatives were prepared and assayed as inhibitors of three carbonic anhydrase (CA) isozymes, hCA I, hCA II and bCA IV [14].
• Installation of a furan carboxylic acid fragment onto a low-micromolar sulfamide resulted in a 23-fold improvement in activity, providing a sub-micromolar, nonpeptidic IL-2 inhibitor (IC(50)=0.60 microM) [12].
• Potent and selective, sulfamide-based human beta 3-adrenergic receptor agonists [15].
• Design, synthesis, and in vitro evaluation of inhibitors of human leukocyte elastase based on a functionalized cyclic sulfamide scaffold [16].
• Tyrosyl sulfamide derivatives as ligands for affinity adsorption of anti FVIII antibodies [17].

References