2038-03-1Relevant articles and documents
SYNTHESIS, STRUCTURE, AND ACTION OF SOME GOSSYPOL DERIVATIVES ON THE PEROXIDATION OF THE LIPIDS OF BIOSUBSTRATES
Dalimov, D. N.,Mukhamedzhanova, E. N.,Shneivais, V. B.,Biktimirov, L.,Ismailov, A. I.,Kamaev, F. G.
, p. 603 - 607 (1989)
The synthesis has been effected of new gossypol derivatives using piperidino- and morpholinoethylamines.According to their PMR spectra, these substances exist in the keto-amine form.Their action on the peroxidation of lipids (POL) of various biosubstrates has been studied.Gossypol bis(piperidinoethylimine) and bis(morpholinoethylimine) in concentrations of 1*1E-7 - 5*1E-6 mM exert a pronounced antioxidant action on human blood serum and rat brain synaptosomes.In the same concentrations, these substances suppressed the POL in enzymatic and nonenzymatic systems of the oxidation of rat liver microsomes.
COMPOUND INHIBITING BUTYRYLCHOLINESTERASE
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Page/Page column 9, (2020/07/31)
The invention concerns a compound according to formula (I), wherein 3 n 11, wherein R comprises or consists of a heterocycle comprising one tertiary amino group providing the binding of R to the rest of the molecule and at least three carbon atoms, wherein all carbon atoms of the heterocycle are unsubstituted or wherein R is a fused bicyclic compound comprising the heterocycle and one further cyclic compound.
Highly Selective Butyrylcholinesterase Inhibitors with Tunable Duration of Action by Chemical Modification of Transferable Carbamate Units Exhibit Pronounced Neuroprotective Effect in an Alzheimer's Disease Mouse Model
Hoffmann, Matthias,Stiller, Carina,Endres, Erik,Scheiner, Matthias,Gunesch, Sandra,Sotriffer, Christoph,Maurice, Tangui,Decker, Michael
, p. 9116 - 9140 (2019/11/03)
In this study, the carbamate structure of pseudo-irreversible butyrylcholinesterase (BChE) inhibitors was optimized with regard to a longer binding to the enzyme. A set of compounds bearing different heterocycles (e.g., morpholine, tetrahydroisoquinoline, benzimidazole, piperidine) and alkylene spacers (2 to 10 methylene groups between carbamate and heterocycle) in the carbamate residue was synthesized and characterized in vitro for their binding affinity, binding kinetics, and carbamate hydrolysis. These novel BChE inhibitors are highly selective for hBChE over human acetycholinesterase (hAChE), yielding short-, medium-, and long-acting nanomolar hBChE inhibitors (with a half-life of the carbamoylated enzyme ranging from 1 to 28 h). The inhibitors show neuroprotective properties in a murine hippocampal cell line and a pharmacological mouse model of Alzheimer's disease (AD), suggesting a significant benefit of BChE inhibition for a disease-modifying treatment of AD.