Phytochemical Profiling of Ephedra alata subsp. alenda Seeds by High-Performance Liquid Chromatography—Electrospray Ionization—Quadrupole-Time-of-Flight-Mass Spectrometry (HPLC-ESI-QTOF-MS), Molecular Docking, and Antioxidant, Anti-diabetic, and Acetylcholinesterase Inhibition

Since the discovery of the cholinergic deficit in Alzheimer disease (AD), acetylcholinesterase (AChE) has been widely investigated in tissues involved in the disease. These studies showed modifications in AChE activity and changes in its polymorphism in brain as well as in cerebro-spinal fluid (CSF) and blood. The co-localization of the enzyme in the senile plaque provided evidence of its anomalous features. It has been also shown that AChE forms a stable complex with senile plaque components through its peripheral anionic site. Moreover, the neurotoxicity of amyloid components is increased by the presence of AChE. The occurrence of an altered glycosylation of some AChE forms in AD is closely related to the presence of amyloid formations. Literature on expression, relationships and modifications in the molecular polymorphism of AChE, in brain, CSF and blood in AD is reviewed.