2548-29-0Relevant articles and documents
3-Functionalised benzenesulphonamide based 1,3,4-oxadiazoles as selective carbonic anhydrase XIII inhibitors: Design, synthesis and biological evaluation
Swain, Baijayantimala,Abhay,Singh, Priti,Angeli, Andrea,Aashritha, Kamtam,Nagesh, Narayana,Supuran, Claudiu T.,Arifuddin, Mohammed
, (2021/02/27)
A new series of benzenesulphonamide linked-1,3,4-oxadiazole hybrids (6a–s) has been synthesized and tested for their carbonic anhydrase inhibition against human (h) carbonic anhydrase (CA) isoforms hCA I, II, IX, and XIII. Fluorescence properties of some of the synthesized molecules were studied. Most of the molecules exhibited significant inhibitory power, comparable or better than the standard drug acetazolamide (AAZ) on hCA XIII. Out of 19 tested molecules, compound 6e (75.8 nM) was 3 times more potent than AAZ (250.0 nM) against hCA I, whereas compound 6e (15.4 nM), 6g (16.2 nM), 6h (16.4 nM) and 6i (17.0 nM) were found to be more potent than AAZ (17.0 nM) against isoform hCA XIII. It is anticipated that these compounds could be taken as the potential leads for the development of selective hCA XIII isoform inhibitors with improved potency.
Synthesis, 3D-structure and stability analyses of NRPa-308, a new promising anti-cancer agent
Brachet, Etienne,Dumond, Aurore,Liu, Wang-Qing,Fabre, Marie,Selkti, Mohamed,Raynaud, Fran?oise,Hermine, Olivier,Benhida, Rachid,Belmont, Philippe,Garbay, Christiane,Lepelletier, Yves,Ronco, Cyril,Pagès, Gilles,Demange, Luc
supporting information, (2019/11/21)
We report herein the synthesis of a newly described anti-cancer agent, NRPa-308. This compound antagonizes Neuropilin-1, a multi-partners transmembrane receptor overexpressed in numerous tumors, and thereby validated as promising target in oncology. The p
Identification and Optimization of Anthranilic Acid Based Inhibitors of Replication Protein A
Patrone, James D.,Pelz, Nicholas F.,Bates, Brittney S.,Souza-Fagundes, Elaine M.,Vangamudi, Bhavatarini,Camper, Demarco V.,Kuznetsov, Alexey G.,Browning, Carrie F.,Feldkamp, Michael D.,Frank, Andreas O.,Gilston, Benjamin A.,Olejniczak, Edward T.,Rossanese, Olivia W.,Waterson, Alex G.,Chazin, Walter J.,Fesik, Stephen W.
supporting information, p. 893 - 899 (2016/05/09)
Replication protein A (RPA) is an essential single-stranded DNA (ssDNA)-binding protein that initiates the DNA damage response pathway through protein-protein interactions (PPIs) mediated by its 70N domain. The identification and use of chemical probes that can specifically disrupt these interactions is important for validating RPA as a cancer target. A high-throughput screen (HTS) to identify new chemical entities was conducted, and 90 hit compounds were identified. From these initial hits, an anthranilic acid based series was optimized by using a structure-guided iterative medicinal chemistry approach to yield a cell-penetrant compound that binds to RPA70N with an affinity of 812 nm. This compound, 2-(3- (N-(3,4-dichlorophenyl)sulfamoyl)-4-methylbenzamido)benzoic acid (20 c), is capable of inhibiting PPIs mediated by this domain.
