Synonyms:Acylcholineacylhydrolase; Benzoylcholinesterase; Butyrylcholine esterase;Butyrylcholinesterase; Choline esterase; Cholinesterase; E.C. 3.1.1.8; E.C.3.1.1.9; Esterase, butyrylcholine; Propionylcholinesterase; Protexia;Pseudocholinesterase
98%,99%, *data from raw suppliers
Butyrylcholinesterase *data from reagent suppliers
The research focuses on the design, synthesis, and evaluation of 2,6-di(substitutedphenyl)thiazolo[3,2-b]1,2,4-triazoles as potential inhibitors of α-amylase, α-glucosidase, and butyrylcholinesterase (a-BuChE), which are relevant in the treatment of type 2 diabetes and Alzheimer's disease. The study involves the synthesis of ten heterocyclic derivatives using phosphorous oxychloride (POCl?) as a cyclization agent. The synthesized compounds were characterized using FTIR, EI-MS, 1H NMR, and 13C NMR techniques. The inhibitory activities of these compounds were tested in vitro, with compound 5c showing strong α-amylase inhibitory activity (IC?? = 1.1 mmol/g), compound 5g demonstrating excellent α-glucosidase inhibition (IC?? = 1.2 mmol/g), and compound 5i being the most potent against a-BuChE (IC?? = 1.5 mmol/g). Molecular docking studies were conducted to understand the binding interactions of these compounds with the target enzymes, revealing key residues involved in binding. Additionally, QSAR models were developed to correlate molecular properties with inhibitory activities, and pharmacokinetic properties were analyzed to assess the drug-likeness of the synthesized compounds. The research highlights the potential of these thiazolo[3,2-b]1,2,4-triazoles as multi-target inhibitors for the treatment of metabolic disorders and neurodegenerative diseases.
This study reports the design, synthesis, biological evaluation, and molecular modeling of a series of substituted pyrrolo[2,1-a]isoquinolinone derivatives as potent inhibitors of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). The researchers used rivastigmine as a starting structure and, through molecular modeling techniques including docking, molecular dynamics simulations, and QTAIM calculations, designed new ligands with stronger inhibitory effects. The synthesis of these compounds was carried out, and their inhibitory activities against AChE and BChE were evaluated. The results showed that compounds 7, 8, and 13 exhibited strong inhibitory activities against both enzymes, with some of them being more potent than rivastigmine. Compound 14 showed selective inhibitory activity against BChE. The molecular modeling study provided insights into the interactions between the ligands and the enzymes, highlighting the importance of interactions with the catalytic anionic site (CAS) and peripheral anionic site (PAS) for the inhibitory effects. The study aims to contribute to the development of new therapeutic options for Alzheimer's disease by identifying and characterizing these novel inhibitors.
The study explores the potential of N-methylpiperidinyl thioesters as surrogate substrates for evaluating corresponding ester compounds as imaging agents for acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) in neurological disorders like Alzheimer's disease. The researchers synthesized various N-methylpiperidinyl thioesters and esters, including derivatives from aryl acid chlorides (4-cyanobenzenecarbothioate, 4-fluorobenzenecarbothioate, and 4-iodobenzenecarbothioate) and alkyl acid chlorides (ethanethioate, propanethioate, and butanethioate), as well as their corresponding esters. These compounds were used to conduct enzyme kinetics studies to determine their affinities and hydrolysis rates by AChE and BuChE. The thioesters were also employed in histochemical evaluations to visualize cholinesterase activity in human brain tissue. The results showed that the thioesters had comparable affinities to their ester counterparts and could effectively visualize cholinesterase distribution in brain tissue, suggesting their potential as screening tools for developing imaging agents targeting the cholinergic system.
The research aims to develop a versatile synthetic approach to create analogs of physovenine and physostigmine, which are known acetylcholinesterase (AChE) inhibitors used in treating conditions like myasthenia gravis, glaucoma, and Alzheimer's disease. The study's purpose is to establish structure-activity relationships (SAR) among these analogs to understand their inhibitory activities against human AChE and butyrylcholinesterase (BuChE). The synthesis process involves multiple steps, including radical cyclization to form the spiro-oxindole ring, acetylation, N-alkylation, and reductive radical cyclization. The most potent analogs identified were 21a with an IC50 value of 70 nM against hBuChE and 21g with an IC50 value of 53 nM against hAChE. The study concludes that the size of the substituent at the quaternary carbon center significantly affects the inhibitory activity against hAChE, with smaller alkyl substituents generally yielding more active compounds. Conversely, larger arylalkyl substituents were more effective against hBuChE. This work provides valuable insights into the SAR of physovenine and physostigmine analogs, guiding future drug design efforts.
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