50623-00-2Relevant articles and documents
Metal-Free Sustainable Synthesis of Amides via Oxidative Amidation Using Graphene Oxide as Carbocatalyst in Aqueous Medium
Dandia, Anshu,Parihar, Sonam,Saini, Pratibha,Rathore, Kuldeep S.,Parewa, Vijay
, p. 3169 - 3175 (2019/07/30)
Abstract: We describe an efficient, clean and metal-free procedure for the synthesis of amides via oxidative amidation of aldehydes with anilines using graphene oxide (GO) as a recyclable catalyst and KBrO3 as a mild oxidant in aqueous medium under microwave irradiation. GO nanosheets were prepared and characterized by XRD, TEM, SEM, and FT-IR, analyses. GO showed high compatibility with KBrO3 in water and offered high TOF value (1.30 × 10?3 mol?g?1 min?1). GO oxygen functionalities catalyze the oxidative amidation effectively in mild condition with high recyclability. A plausible mechanism was proposed by the isolating the intermediate. Graphic Abstract: [Figure not available: see fulltext. ]
Scaffold identification of a new class of potent and selective BCRP inhibitors
Marighetti, Federico,Steggemann, Kerstin,Karbaum, Maria,Wiese, Michael
, p. 742 - 751 (2015/04/14)
We recently reported the synthesis and quantitative structure-activity relationships of a new breast cancer resistance protein (BCRP) inhibitor class. In the study presented herein, we investigated the possibility to better define the scaffold of this compound class by removing or modifying the aromatic ring A with various substituents selected on the basis of their electronic and lipophilic properties. The results show that this aromatic ring is important, but not essential, for activity. Many of the selected substituents led to compounds with low activity, but in some cases activity was retained. Among these, a phenolic hydroxy group proved to impart as much potency to the molecule as a hydroxyethyl side chain, initially considered necessary for activity. This derivative is one of the most active compounds in this class, maintaining an inhibitory activity similar to that of the reference compound; it is also selective for BCRP.
Inhibition studies on Mycobacterium tuberculosis N-acetylglucosamine-1- phosphate uridyltransferase (GlmU)
Tran, Anh Thu,Wen, Daying,West, Nicholas P.,Baker, Edward N.,Britton, Warwick J.,Payne, Richard J.
supporting information, p. 8113 - 8126 (2013/12/04)
Peptidoglycan is an essential component of the cell wall of bacteria, including Mycobacterium tuberculosis, that provides structural strength and rigidity to enable internal osmotic pressure to be withstood. The first committed step in the biosynthesis of peptidoglycan involves the formation of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) from uridine triphosphate (UTP) and GlcNAc-1-phosphate. This reaction is catalysed by N-acetylglucosamine- 1-phosphate uridyltransferase (GlmU), a bifunctional enzyme with two independent active sites that possess acetyltransferase and uridyltransferase activities. Herein, we report the first inhibition study targeted against the uridyltransferase activity of M. tuberculosis GlmU. A number of potential inhibitors were initially prepared leading to the discovery of active aminoquinazoline-based compounds. The most potent inhibitor in this series exhibited an IC50 of 74 μM against GlmU uridyltransferase activity and serves as a promising starting point for the discovery of more potent inhibitors.
