2014
DOI: 10.1016/j.jmgm.2014.09.002
|View full text |Cite
|
Sign up to set email alerts
|

Ab initio molecular simulations for proposing potent inhibitors to butyrylcholinesterases

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
11
0

Year Published

2016
2016
2021
2021

Publication Types

Select...
6

Relationship

0
6

Authors

Journals

citations
Cited by 9 publications
(11 citation statements)
references
References 28 publications
0
11
0
Order By: Relevance
“…Similarly, at the BChE active site, 2 bound with Tyr332 within the anionic hinge that prevents choline from entering the enzyme cavity. A recent study by Murakawa et al 38 revealed that Phe329 is a common binding site for active BChE inhibitors. The authors also described that Asp70 in the hinge and Gly116 within the oxyanion cavity form another active site for BChE where inhibitors may bind.…”
Section: Discussionmentioning
confidence: 99%
“…Similarly, at the BChE active site, 2 bound with Tyr332 within the anionic hinge that prevents choline from entering the enzyme cavity. A recent study by Murakawa et al 38 revealed that Phe329 is a common binding site for active BChE inhibitors. The authors also described that Asp70 in the hinge and Gly116 within the oxyanion cavity form another active site for BChE where inhibitors may bind.…”
Section: Discussionmentioning
confidence: 99%
“…In a later study of six inhibitors binding to the same enzyme, they obtained a somewhat poorer correlation (R 2 = 0.72, without entropy correction), 290 and the correlation was even worse for the binding of four ligands to butylcholinesterase (still without any entropy correction), R 2 = 0.54. 291 Explicit water molecules have also been included in studies of the plasminogen activator 292 and the 2G12 antibody. 293 They often gave unrealistically large absolute binding energies, because fixed water molecules underestimate the electrostatic screening.…”
Section: Fmomentioning
confidence: 99%
“…They obtained a good correlation to the experimental data ( R 2 = 0.94), but the absolute affinities were ∼20 times larger than the experimental ones. In a later study of six inhibitors binding to the same enzyme, they obtained a somewhat poorer correlation ( R 2 = 0.72, without entropy correction), and the correlation was even worse for the binding of four ligands to butylcholinesterase (still without any entropy correction), R 2 = 0.54 . Explicit water molecules have also been included in studies of the plasminogen activator and the 2G12 antibody .…”
Section: Single-structure Approachesmentioning
confidence: 99%
“…In the healthy brain, acetylcholinesterase (AChE) is the most important enzyme regulating the level of ACh, while butyrylcholinesterase (BChE) plays a minor role [ 1 ]. It is therefore expected that if the hydrolysis of ACh by AChE and BChE is inhibited in the brain of an AD patient, the amount of ACh in the synapse will be significantly increased and the neurotransmission mechanism will be more fluid [ 9 ]. For this reason, acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) inhibitors such as galantamine, donepezil, and rivastigmine are used in the management of AD, and the inhibition of the two types of cholinesterase enzymes (AChE and BuChE) as remedial for such treatment [ 10 ].…”
Section: Introductionmentioning
confidence: 99%