This product is isolated and purified from the bulbs of Lycoris radiata
(4aS,6R,8aS)-3-Methoxy-11-methyl-5,6,9,10,11,12-hexahydro-4aH-benzofuro[3a,3,2-ef]benzazepin-6-olhydrobromid/NIVALIN,HBR/(4aS,6R,8aS)-3-methoxy-11-methyl-5,6,9,10,11,12-hexahydro-4aH-benzofuro[3a,3,2-ef]benzazepin-6-ol hydrobromide/(4aS,6R,8aS)-3-methoxy-11-methyl-5,6,9,10,11,12-hexahydro-4aH-benzofuro[3a,3,2-ef]benzazepin-6-ol bromhydrate/Galanthamine hydrobromide (1:1)/GALANTHAMIDE HYDROBROMIDE/[3H]-Galantamine hydrobromide/galanthamine bromhydrate (1:1)/Galantamine hydrobromide (JAN/USAN)/Galanthamine HBr/Galanthamine (hydrobromide)/Galantamine hydrobromide/(-)-Galanthaminium bromide/NIVALIN/6H-Benzofuro[3a,3,2-ef]benzazepin-6-ol, 4a,5,9,10,11,12-hexahydro-3-methoxy-11-methyl-, (4aS,6R,8aS)-, hydrobromide (1:1)/galanthaminhydrobromid(1:1)/GALANTHAMINE HYDROBROMIDUM/GALANTAMINE HBR/6H-benzofuro[3a,3,2-ef]benzazepin-6-ol, 4a,5,9,10,11,12-hexahydro-3-methoxy-11-methyl-, (4aS,6R,8aS)-, hydrobromide
J Pharm Biomed Anal. 2011 Apr 28;55(1):85-92. Stability-indicating study of the anti-Alzheimer's drug galantamine hydrobromide.[Pubmed: 21300511]Galantamine hydrobromide was subjected to different stress conditions (acidic, alkaline, thermal, photolytic and oxidative). Degradation was found to occur under acidic, photolytic and oxidative conditions, while the drug was stable under alkaline and elevated temperature conditions. METHODS AND RESULTS:A stability-indicating reversed-phase liquid chromatographic method was developed for the determination of the drug in the presence of its degradation products. The method was validated for linearity, precision, accuracy, specificity, selectivity and intermediate precision. Additionally, the degradation kinetics of the drug was assessed in relevant cases. The kinetics followed a first order behavior in the case of acidic and photolytic degradation, while a two-phase kinetics behavior was found for the oxidative degradation. CONCLUSIONS: The degradation products were characterized by mass spectrometry and nuclear magnetic resonance spectroscopy. Dehydration, epimerization and N-oxidation were the main processes observed during the degradation of galantamine. Moreover, if sufficient material could be isolated the inhibitory activity against the target enzyme acetylcholinesterase was also assessed.
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Introduction: Alzheimer’s disease (AD) is the most common cause of major neurocognitive disorders with a prevalence in the US of about 5.7 million in 2018. With the disease burden projected to increase dramatically in the coming years, it is imperative to review the current available treatment regimens for their safety and utility. The cholinesterase inhibitors (ChEIs) have continued to play a pivotal role in managing the symptoms and possibly slowing the rate of progression of AD since 1993. Owing to their being a mainstay in the treatment of AD, the safety and efficacy of prescribing these drugs needs to be reviewed often, especially with the approval of new formulations and doses.Areas covered: The three ChEIs currently approved by the FDA are donepezil, rivastigmine and galantamine. This article will review the safety and tolerability of these ChEIs and analyze the potential disease modifying properties of these drugs. The authors have reviewed all recent literature including review articles, meta-analyzes, clinical trials and more.Expert opinion: These ChEIs differ subtly in their mechanisms of action, in their tolerability and safety and FDA-approved indications. All are considered first-line, symptomatic treatments of the various phases of AD and may even have potentially disease-modifying effects.
Alzheimer’s disease treatment; adverse effects; cholinesterase inhibitors; donepezil; galantamine; rivastigmine; safety of cholinesterase inhibitors; side effects; symptomatic treatment for Alzheimer’s disease
An update on the utility and safety of cholinesterase inhibitors for the treatment of Alzheimer's disease.
Haake A1, Nguyen K1, Friedman L2, Chakkamparambil B1, Grossberg GT1.
Non-specific binding of a fluorescent probe to human serum albumin is problematic because it induces signal interference when the probe detects the target biomarker in human serum. To eliminate this problem, we used intrinsically problematic non-specific fluorescence in designing a fluorescent probe for butyrylcholinesterase activity in serum. The probe containing a fluorophore with specific binding affinity for albumin could sensitively detect butyrylcholinesterase activity in serum with high selectivity to acetylcholinesterase and screen the efficiency of butyrylcholinesterase inhibitors.
A fluorescent probe for butyrylcholinesterase activity in human serum based on a fluorophore with specific binding affinity for human serum albumin.
Yoo S1, Han MS1.
2019 Dec 18
A high-performance liquid chromatography-mass spectrometry technique hyphenated on-line with an immobilized enzyme reactor (IMER) was developed by the use of 3 known acetylcholinesterase (AChE) inhibitors (galanthamine, huperzine A and tacrine). This bioanalytical device allows qualitative comparison of the inhibitory strengths of AChE inhibitors. The AChE inhibitory strengths were evaluated and compared by the corresponding acetylcholine peak areas (mass signal) obtained after a chromatographic separation and the elution through the IMER. Only one injection of the analytes is needed to get this comparative analysis. This bioanalytical device was then applied to the extract of a natural plant, Lycoris radiata, which is known to contain AChE inhibitors such as galanthamine and lycoramine. Aside from the demonstration of the inhibitory activity of the two known AChE inhibitors, the AChE inhibitory activity of another compound (dihydro-latifaliumin C) was revealed. This is the first report describing the AChE inhibitory activity of this compound.
Copyright © 2019. Published by Elsevier B.V.
Acetylcholinesterase inhibitor; Alkaloid; Bioanalytical device; Immobilized enzyme reactor; MS
Online acetylcholinesterase inhibition evaluation by high-performance liquid chromatography-mass spectrometry hyphenated with an immobilized enzyme reactor.
Yuan Y1, Zhao M1, Riffault-Valois L1, Ennahar S1, Bergaentzle M1, Marchioni E2.
2020 Jan 4