246544-91-2

Upstream product

• 24165-03-5 tritylsulfenyl chloride 
• 51-45-6 histamine 
• 246544-90-1 4,5,6,7-tetrabromo-2-[2-(1-tritylsulfanyl-1H-imidazol-4-yl)-ethyl]-isoindole-1,3-dione 

Downstream Products

• 317810-02-9 C₃₂H₃₀N₄O₃S₂ 

Relevant academic research and scientific papers

Carbonic anhydrase activators: Part 24. High affinity isozymes I, II and IV activators, derivatives of 4-(4-chlorophenylsulfonylureido-amino acyl)ethyl-1H-imidazole

N-1-Tritylsulfenyl histamine was synthesized by reaction of histamine (Hst) with tetrabromophthalic anhydride followed by protection of its imidazole moiety with tritylsulfenyl chloride. After hydrazinolysis, it afforded a key intermediate which was deriv

Carbonic anhydrase activators - Part 21. Novel activators of isozymes I, II and IV incorporating carboxamido and ureido histamine moieties

Reaction of histamine with tetrabromophthalic anhydride and protection of its imidazole moiety with tritylsulfenyl chloride, followed by hydrazinolysis, afforded N-1-tritylsulfenyl histamine, a key intermediate which was further derivatized at its aminoethyl moiety. Carboxamido derivatives were obtained by reaction of the key intermediate with carboxylic acid anhydrides, acyl chlorides or carboxylic acids in the presence of carbodiimides. Reaction of the same key intermediate with isocyanates, isothiocyanates, cyanamide or dicyandiamide afforded another series of compounds. Deprotection of the above-mentioned intermediates with hydrochloric acid in dioxane afforded two series of compounds, histamine derivatives possessing carboxamido, ureido, thioureido or guanidino moieties in their molecule. The new derivatives were assayed as activators of three carbonic anhydrase (CA) isozymes, hCA I, hCA II (cytosolic forms) and bCA IV (membrane-bound form, h = human, b = bovine isozyme). Efficient activation was observed against all three isozymes, but especially against hCA I and bCA IV, with affinities in the nanomolar range for the best compounds. hCA II was, on the other hand, activatable with affinities around 10-25 nM. This new class of CA activators might lead to the development of drugs/diagnostic agents for the CA deficiency syndrome, a genetic disease of bone, brain and kidneys. (C) 2000 Editions scientifiques et medicales Elsevier SAS.

Carbonic anhydrase activators: Amino acyl/dipeptidyl histamine derivatives bind with high affinity to isozymes I, II and IV and act as efficient activators

Reaction of histamine (Hst) with tetrabromophthalic anhydride and protection of its imidazole moiety with tritylsulfenyl chloride, followed by hydrazinolysis, afforded N-1-tritylsulfenyl-histamine, a key intermediate which was further derivatized at its aminoethyl moiety. Reaction of the key intermediate with N-Boc-amino acids/dipeptides (Boc-AA) in the presence of carbodiimides afforded, after deprotection of the imidazolic and amino moieties, a series of compounds with the general formula AA-Hst (AA=amino acyl; dipeptidyl). The new derivatives were assayed as activators of three carbonic anhydrase (CA) isozymes, hCA I, hCA II (cytosolic forms) and bCA IV (membrane-bound form). Efficient activation was observed against all three isozymes, but especially against hCA I and bCA IV, with affinities in the nanomolar range for the best compounds. hCA II was, on the other hand, activatable with affinities around 10-20 nM. This new class of CA activators might lead to the development of drugs/diagnostic agents for the CA deficiency syndrome, a genetic disease of bone, brain and kidneys. Copyright (C) 1999 Elsevier Science Ltd.

Novel carbonic anhydrase isozymes I, II and IV activators incorporating sulfonyl-histamino moieties

Sulfonylamido(ureido) derivatives of histamine were synthesized by an original procedure in order to obtain tight-binding activators of the zinc enzyme carbonic anhydrase (CA), exploiting the binding energy of the alkyl/arylsulfonyl moieties with amino acid residues at the entrance of the active site. In contrast to the lead molecule, histamine, the new derivatives possessed higher affinity for three different CA isozymes, as evidenced by compairing the affinity constants of these compounds for isozyme CA II.