80707-14-8Relevant academic research and scientific papers
Catalytic Redox Chain Ring Opening of Lactones with Quinones to Synthesize Quinone-Containing Carboxylic Acids
Xu, Xiao-Long,Li, Zhi
supporting information, p. 5078 - 5081 (2019/09/03)
Catalytic ring opening of five- to eight-membered lactones with quinones is achieved through a redox chain mechanism. With low loading of a simple metal triflate Lewis acid catalyst and a chain initiator, C-H bonds of many quinones were efficiently functionalized with carboxylic acid-containing side chains. This method also features 100% atom economy and wide substrate scope. A novel route to the anti-asthma drug Seratrodast was developed. Mechanism study suggests that the redox chain reaction likely undergoes a carbocation intermediate.
Novel high-affinity and selective biaromatic 4-substituted γ-hydroxybutyric acid (GHB) analogues as GHB ligands: Design, synthesis, and binding studies
H?g, Signe,Wellendorph, Petrine,Nielsen, Birgitte,Frydenvang, Karla,Dahl, Ivar F.,Br?uner-Osborne, Hans,Brehm, Lotte,Fr?lund, Bente,Clausen, Rasmus P.
experimental part, p. 8088 - 8095 (2009/12/07)
γ-Hydroxybutyrate (GHB) is a metabolite of γ-aminobutyric acid (GABA) and has been proposed to function as a neurotransmitter or neuromodulator. GHB is used in the treatment of narcolepsy and is a drug of abuse. GHB binds to both GABAB receptors and specific high-affinity GHB sites in brain, of which the latter have not been linked unequivocally to function, but are speculated to be GHB receptors. In this study, a series of biaromatic 4-substituted GHB analogues, including 4′-phenethylphenyl, 4′-styrylphenyl, and 4′-benzyloxyphenyl GHB analogues, were synthesized and characterized pharmacologically in a [3H](E,RS)-(6,7, 8,9-tetrahydro-5-hydroxy-5H-benzocyclohept-6-ylidene)acetic acid ([ 3H]NCS-382) binding assay and in GABAA and GABA B receptor binding assays. The compounds were selective for the high-affinity GHB binding sites and several displayed Ki values below 100 nM. The affinity of the 4-[4′-(2-iodobenzyloxy)phenyl] GHB analogue 17b was shown to reside predominantly with the R-enantiomer (Ki = 22 nM), which has higher affinity than previously reported GHB ligands.
