Specifically, compound 4g exhibited the potent ability to inhibit cholinesterase (ChE) (IC<sub>50</sub>, 19.7 nM for hAChE and 0.66 μM for hBuChE) and the good Aβ aggregation inhibition (49.2% at 20 μM), and it was also a good antioxidant (1.26 trolox equivalents).
The biological assay results demonstrate the ability of several quinazoline derivatives to inhibit both acetyl and butyrylcholinesterase (AChE and BuChE) enzymes (IC<sub>50</sub> range = 1.6-30.5 μM), prevent beta-amyloid (Aβ) aggregation (IC<sub>50</sub> range 270 nM-16.7 μM) and exhibit antioxidant properties (34-63.4% inhibition at 50 μM).
We have demonstrated that this approach is possible, and that a number of readily available tacrine analogues show cholinesterase inhibition power, as well as other pharmacological properties, such as calcium channel blockade, antioxidant properties, neuroprotection, Aβ-amyloid inhibition aggregation capacity, etc., making them suitable multipotent molecules for further development for the potential treatment of AD.
β-asarone improves learning and memory and reduces Acetyl Cholinesterase and Beta-amyloid 42 levels in APP/PS1 transgenic mice by regulating Beclin-1-dependent autophagy.
Butyrylcholinesterase (BChE) genotypes and protein (BuChE) activity, especially in combination with Apolipoprotein E4 (ApoE4), have been investigated as risk factors for developing Alzheimer disease (AD) and may be associated with the rate of progression of cognitive decline.Despite similar pathologic (e.g. amyloid deposition) and neurochemical (e.g. cholinergic deficits) aspects between AD and Lewy body diseases (LBD), scarce data is obtainable about BChE genotypes and BuChE activity in LBD.
We examined the relationship between the K variant of BuChE and the severity of deposits of amyloid (Abeta(1-42)) and phosphorylated tau in the temporal cortex (BA36) of 30 prospectively studied autopsy-diagnosed dementia (Alzheimer's disease and dementia with Lewy bodies) patients.