20172-97-8Relevant articles and documents
Inhibitors of fumarylacetoacetate hydrolase domain containing protein 1 (Fahd1)
Eder, Manuel Philip,Gstach, Hubert,Jansen-Dürr, Pidder,Klapec, Patrycia,Liedl, Klaus R.,Loeffler, Johannes R.,Monteleone, Stefania,Weiss, Alexander K. H.,Wurzer, Richard,von Grafenstein, Susanne
, (2021/08/26)
FAH domain containing protein 1 (FAHD1) acts as oxaloacetate decarboxylase in mitochondria, contributing to the regulation of the tricarboxylic acid cycle. Guided by a high-resolution X-ray structure of FAHD1 liganded by oxalate, the enzymatic mechanism of substrate processing is analyzed in detail. Taking the chemical features of the FAHD1 substrate oxaloacetate into account, the potential inhibitor structures are deduced. The synthesis of drug-like scaffolds afforded first-generation FAHD1-inhibitors with activities in the low micromolar IC50 range. The investigations disclosed structures competing with the substrate for binding to the metal cofactor, as well as scaffolds, which may have a novel binding mode to FAHD1.
Reagent Design and Ligand Evolution for the Development of a Mild Copper-Catalyzed Hydroxylation Reaction
Fier, Patrick S.,Maloney, Kevin M.
supporting information, p. 3033 - 3036 (2017/06/07)
Parallel synthesis and mass-directed purification of a modular ligand library, high-throughput experimentation, and rational ligand evolution have led to a novel copper catalyst for the synthesis of phenols with a traceless hydroxide surrogate. The mild reaction conditions reported here enable the late-stage synthesis of numerous complex, druglike phenols.
Crystal structure and DNA-binding study of a monoclinic polymorph of N,N′-bis(2-pyridyl)oxamide
Zhang, Wan-Ju,Zhang, Kai,Wang, Fang
, p. 712 - 716 (2015/02/19)
A monoclinic polymorph of N,N′-bis(2-pyridyl)oxamide has been synthesized and characterized by single-crystal X-ray diffract ion method. It crystallizes in monoclinic, space group C2/c with crystallographic data: a = 10.596(3) A, b = 12.950(3) A, c = 8.612(2) A, β = 90.935(8)° and Z = 4. In the polymorph, two-dimensional network is formed by hydrogen bond and π-π stacking interact ion. The binding studies of the compound with calf thymus DNA (CT-DNA) have also been explored by elect ronic absorpt ion t it rat ion and fluorescence quenching experiments, and the results suggest that the compound binds to CT-DNA through groove binding.