20114-85-6Relevant academic research and scientific papers
Molecular docking and investigation of 4-(benzylideneamino)- and 4-(benzylamino)-benzenesulfonamide derivatives as potent AChE inhibitors
I??k, Mesut,Demir, Yeliz,Durgun, Mustafa,Türke?, Cüneyt,Necip, Adem,Beydemir, ?ükrü
, p. 1395 - 1405 (2019/11/16)
The discovery of acetylcholinesterase inhibitors is important for the treatment of Alzheimer’s disease (AD), known as the most common type of dementia. Due to the side effects of commonly used acetylcholinesterase inhibitors, studies for the detection of
Benzenesulfonamide derivatives containing imine and amine groups: Inhibition on human paraoxonase and molecular docking studies
Akku?, Musa,Beydemir, ?ükrü,Demir, Yeliz,Durgun, Mustafa,I??k, Mesut,Nas?r, Abdul,Necip, Adem,Türke?, Cüneyt
, (2019/12/09)
Sulfonamides known as inhibitors of many metabolic enzymes have been widely used as antimicrobial drugs for a long time. In the present study, we investigated in vitro inhibitory activities of benzenesulfonamide derivatives on human paraoxonase-I (hPON1). For this aim, PON1 was purified from human serum with a specific activity of 2603.57 EU/mg and 8.34% yield using simple chromatographic methods. The various concentrations of early-synthesized sixteen sulfonamide derivatives were tested on the paraoxonase activity. Ki values of compounds were found in the range of 0.28–357.70 μM. Compound H4 had the highest inhibitory activity on hPON1 as competitive. Estimated structure–activity relationship (SAR) for compounds was done based on different substituents and their positions in the compounds. Besides, the molecular docking analysis of compound H4 was performed to understand the binding interactions on the active site of the enzyme. According to these experimental results, compound H4 was a potential inhibitor of PON1.
Synthesis of 4-sulfamoylphenyl-benzylamine derivatives with inhibitory activity against human carbonic anhydrase isoforms I, II, IX and XII
Durgun, Mustafa,Turkmen, Hasan,Ceruso, Mariangela,Supuran, Claudiu T.
, p. 982 - 988 (2016/02/19)
Imine derivatives were obtained by condensation of sulfanilamide with substituted aromatic aldehydes. The Schiff bases were thereafter reduced with sodium borohydride, leading to the corresponding amines, derivatives of 4-sulfamoylphenyl-benzylamine. These sulfonamides were investigated as inhibitors of the human carbonic anhydrase (hCA, EC 4.2.1.1) isoforms hCA I and II (cytosolic isozymes), as well as hCA IX and XII (transmembrane, tumor-associated enzymes). We noted that the compounds incorporating secondary amine moieties showed a better inhibitory activity against all CA isozymes compared to the corresponding Schiff bases. Low nanomolar CA II, IX and XII inhibitors were detected, whereas the activity against hCA I was less potent. The secondary amines incorporating sulfonamide or similar zinc-binding groups, poorly investigated chemotypes for designing metalloenzyme inhibitors, may offer interesting opportunities in the field due to the facile preparation and possibility to explore a vast chemical space.
