Abstract
Acetylcholinesterase (AChE) (EC 3.1.1.7) is an important enzyme that breaks down of acetylcholine in synaptic cleft in neuronal junctions. Inhibition of AChE is associated with treatment of several diseases such as Alzheimer's disease (AD), myasthenia gravis, and glaucoma as well as the mechanisms of insecticide and anthelmintic drugs. Several AChE inhibitors are available in clinical use currently for the treatment of AD; however, none of them has ability, yet, to seize progress of the disease. Consequently, an extensive research has been going on finding new AChE inhibitors. In this sense, natural inhibitors have gained great attention due to their encouraging effects toward AChE. In this review, promising candidate molecules with marked AChE inhibition from both plant and animal sources will be underlined.
Highlights
Acetylcholinesterase (AChE) (EC 3.1.1.7), known as acetylhydrolase, is a serine protease type of enzyme that catalyzes breaking down of acetylcholine (ACh) into choline and acetic acid and terminates neurotransmission at cholinergic synapses
In addition to widerange use of AChE inhibitors towards Alzheimer’s disease (AD), certain chemical classes of pesticides, such as organophosphates and carbamates, work by interfering or inhibiting irreversibly this enyzme, which is expressed in all invertebrate and vertebrate animals as a key enzyme of the cholinergic system [13,14]. Another treatment approach for utilization of AChE inhibitors has been stated against myasthenia gravis (MG) through inhibition of peripheral AChE [15,16], while AChE inhibitors are considered as the third line drugs for the treatment of glaucoma, which have been described to be better agents with fewer local and systemic adverse effects [17]
Since bisdemethoxycurcumin appeared to be more effective than the parent curcuminoids, the authors commented that the additional methoxy group (-OCH3) on the structure of bisdemethoxycurcumin may influence the level of AChE inhibitory activity
Summary
Acetylcholinesterase (AChE) (EC 3.1.1.7), known as acetylhydrolase, is a serine protease type of enzyme that catalyzes breaking down of acetylcholine (ACh) into choline and acetic acid and terminates neurotransmission at cholinergic synapses. For instance; two new [6,7epoxy-3,5,20-trihydroxy-1-oxowitha-24-enolide (1) and 5,6-epoxy-4,17,27-trihydroxy-1-oxowitha-2,24-dienolide (2)] and four known withanolides [withaferin A (3), 2,3dihydrowithaferin-A (4), 6,7-epoxy-5,20-dihydroxy-1oxowitha-2,24-dienolide (5), and 5,6-epoxy-4-hydroxy1-oxowitha-2,14,24-trienolide (6)] isolated from the methanol extract of W. somnifera collected in Karachi (Pakistan) were tested for their possible AChE inhibitory effect and only four of the compounds, whose IC50 values varied between 50±2.0 and 161.5±1.1 μM, were found to display moderate level of inhibition towards AChE as compared to galanthamine (IC50 = 0.50±0.001 μM) employed as the reference [30].
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