Butyrylcholinesterase

Recent Findings on butyrylcholinesterase

• Eugenol-derived carbamates were investigated as potential dual cholinesterase inhibitors with neuroprotective activity relevant to Alzheimer’s disease. The lead compound E10 showed a “genuine dual inhibitory profile,” with an AChE IC50 of 4.25 nM and a BChE IC50 of 3.20 nM, supporting its characterization as a potent dual-target candidate for different disease stages 42442298Jul. The study focused on structure–activity relationships and molecular dynamics insights, linking compound optimization with computational analysis of ligand–protein interactions.

• A series of 2-indolinone benzylpiperidine–thiosemicarbazone hybrids was designed, synthesized, and evaluated for cholinesterase inhibition. The compounds were compared with donepezil, which was reported in the study to have an IC50 of 0.44 μM against AChE and 4.70 μM against BuChE 42372459Jun. This work therefore used BChE inhibition as one component of a comparative anti-cholinesterase assessment rather than evaluating the enzyme in isolation.

• Dispiroindene–pyrrolidinedione scaffolds were developed as multi-target-directed ligands combining AChE inhibition with antioxidant activity and favorable biocompatibility in SH-SY5Y cells. The compound series also showed notable affinity for BChE, with several derivatives displaying submicromolar to low-micromolar inhibition 42462519Jul. The study extended BChE-focused medicinal chemistry toward compounds intended to combine cholinesterase inhibition with cellular and antioxidant properties.

• Cyclopropyl-appended thiohydantoin derivatives were designed as dual cholinesterase and COX inhibitors. The investigation combined experimental synthesis and biological evaluation with DFT calculations, molecular docking, and molecular dynamics simulations. Computational analyses indicated favorable electronic properties and stable ligand–protein complex formation at the active sites of AChE, BChE, and COX-2 42726329Sep. BChE was therefore incorporated into a multitarget framework that also addressed inflammatory signaling and antioxidant-related drug-design objectives.

• Piperidine-based chalcones were synthesized by a microwave-assisted method and evaluated against MAO-A, MAO-B, AChE, and BChE in a study directed toward anti-Parkinson potential. The work examined a library of 27 compounds and used BChE as part of a broader enzyme-inhibition profile alongside MAO-B and AChE 42190536May. The supplied publication context identifies the study’s screening strategy but does not specify a BChE potency value for an individual compound.

• Novel chalcone derivatives containing benzoyl-piperazine were studied through synthesis, biological testing, ADMET profiling, molecular docking, network pharmacology, and molecular dynamics simulation. Compound 2q was identified as the most promising candidate in the reported series, showing the strongest inhibitory activities against AChE and BChE together with anti-inflammatory effects 42166963May. The study illustrates the use of BChE inhibition as one element of a combined neurodegenerative and inflammatory pharmacology profile.

• β-Maltose-conjugated acetophenone thiosemicarbazones were evaluated as multitarget inhibitors of enzymes associated with diabetes and Alzheimer’s disease. The compounds were tested against α-amylase, α-glucosidase, AChE, and BChE 42184581May. This design connected BChE inhibition with carbohydrate-metabolism targets, broadening the multi-target strategy beyond cholinergic enzymes alone.

• Benzimidazol-2-one hybrids incorporating piperazine, coumarin, and triazole moieties were designed and synthesized as potential anti-Alzheimer’s disease agents. Their biological evaluation included inhibition assays against AChE, BChE, and MAO-B, together with antioxidant-potential measurements using online HPLC-based assays 42623026Aug. BChE was thus assessed alongside a second cholinesterase, a monoamine oxidase target, and oxidative-stress-related pharmacology.

• Sulfonamide-based 2-amino-1,3,4-oxadiazole derivatives were investigated as dual cholinesterase and carbonic anhydrase inhibitors. Their activities were evaluated against AChE, BChE, carbonic anhydrases I and II, and α-glucosidase, with the study also incorporating kinetic characterization, molecular modeling, and ADMET evaluation 42638586Aug. This work positioned BChE within a broader enzyme-targeting program that combined cholinesterase inhibition with carbonic anhydrase and glycosidase inhibition.

• Collectively, these publications extend the dominant literature theme of multi-target neurodegenerative therapy. Across the reported studies, BChE is repeatedly paired with AChE and, in different chemical series, with MAO-B, COX-2, carbonic anhydrases, α-amylase, or α-glucosidase. Molecular docking and molecular dynamics simulations are used to interpret binding and complex stability, while antioxidant activity, oxidative-stress assays, cellular biocompatibility, and ADMET profiling are used to complement enzyme inhibition. The results support continued exploration of BChE-directed compounds as multifunctional lead structures, but the provided studies report medicinal-chemistry and preclinical evaluation rather than demonstrated clinical benefit.