65782-57-2Relevant academic research and scientific papers
Zinc oxide catalyzed solvent-free mechanochemical route for C-S bond construction: A sustainable process
Md. Khaja Mohinuddin,Gangi Reddy
, p. 1207 - 1214 (2017)
A zinc oxide catalyzed solvent-free mechanochemical process has been developed for the rapid construction of C-S bonds by using a nucleophilic substitution reaction (SN2 mechanism) that involves a variety of thiols and phenacyl/ benzyl/alkyl bromides. Notable advantages of this method in-clude its broad substrate scope, clean reaction profile, safety, scalability, high product yields at ambient conditions, and the recyclability of the catalyst. Furthermore, the prepared compounds are valuable building blocks for the synthesis of various biologically active molecules.
Developing a scaffold for urease inhibition based on benzothiazoles: Synthesis, docking analysis, and therapeutic potential
?zil, Musa,Tuzcuo?lu, ?zge,Emirik, Mustafa,Balta?, Nimet
, (2021/09/25)
The synthesis, in silico molecular docking, and in vitro urease inhibition studies of a novel series of benzothiazole derivatives are reported. The title compounds in the two series, namely, 2-({5-[(benzothiazol-2-ylthio)methyl]-1,3,4-oxadiazol-2-yl}thio)-1-(4-substituted-phenyl)ethan-1-one and 2-(benzothiazol-2-ylthio)-1-(4-substituted-phenyl)ethan-1-one oxime, were synthesized by the reaction of benzo[d]thiazole-2-thiol with different kinds of intermediates in several steps using both conventional and microwave techniques. All compounds were found to have an excellent degree of urease-inhibitory potential ranging between 16.16 ± 0.54 and 105.32 ± 2.10 μM when compared with the standard inhibitor acetohydroxamic acid with IC50 = 320.70 ± 4.24 μM. The structure–activity relationship was established in detail. The binding interactions of the compounds with the enzyme were confirmed through molecular docking. Further, 100 -ns molecular dynamics simulations were performed to investigate the stability and structural perturbations experienced by the most potent compound over the urease active site.
