658702-70-6Relevant academic research and scientific papers
Unsymmetrical Cysteine Disulfides as Carbonic Anhydrase Inhibitors
Caira, M.,Hunter, R.,Oztekin, A.,Stellenboom, N.,Zilbeyaz, K.
, p. 1020 - 1027 (2021/10/26)
Abstract: A small library of unsymmetrical cysteine disulfides as four aliphatic, three aromatic and one heteroaromatic were evaluated for their inhibition of two important carbonic anhydrase (CA) enzymes, namely human carbonic anhydrase isoenzymes I (hCA I) and II (hCA II). IC50 values were recorded in the low nanomolar range (8.6–18.3 nM for hCA I and 42.9–99.9 nM for hCA II). The inhibition activities were significantly superior to those of the clinically available CA inhibitor acetazolamide for hCA I, while only marginally inferior for hCA II. These results highlight the relevance of screening small molecules as potential CA inhibitors (CAIs).
The synthesis and reaction of N-sulfenyl heterocycles: Development of effective sulfenylating reagents
Shimizu, Masao,Fukazawa, Hidenori,Shimada, Shigeru,Abe, Yoshimoto
, p. 2175 - 2182 (2007/10/03)
Various N-sulfenyl heterocycles were synthesized by transamination of sulfenamides using a chlorine gas-free method. The N-sulfenyl heterocycles behaved as sulfenylating reagents of anilines; N-sulfenylbenzimidazoles were the most effective.
