Ask about this productRelated genes to: BCHE antibody
- Gene:
- BCHE NIH gene
- Name:
- butyrylcholinesterase
- Previous symbol:
- CHE1, CHE2
- Synonyms:
- E1
- Chromosome:
- 3q26.1
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2016-10-05
Related products to: BCHE antibody
Related articles to: BCHE antibody
- Anthocyanins are water-soluble plant pigments. They give many plants, fruits, vegetables, and cereal kernels their red, purple, and blue colors. This research aims to reveal the biological properties of peonidin as an anthocyanin. To comprehend the antioxidant capabilities of peonidin, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) radical (ABTS), N,N-dimethyl-p-phenylenediamine dihydrochloride radical (DMPD), and 1,1-diphenyl-2-picrylhydrazyl free radical (DPPH) scavenging, Fe-2,4,6-tris(2-pyridyl)-s-triazine (TPTZ), and Cu reducing assays were recorded. The IC values for peonidin against ABTS, DMPD and DPPH scavenging capabilities were determined to compare with standard antioxidants. ABTS radical scavenging activity of peonidin had an IC value of 15.40 μg/mL, while the IC values for BHA, BHT, Trolox, and α-Tocopherol were 12.82, 11.78, 12.67, and 10.83 μg/mL, respectively. DPPH radical scavenging activity of peonidin had an IC value of 41.63 μg/mL, while the IC values for BHA, BHT, Trolox, and α-Tocopherol were 8.45, 23.10, 6.30, and 18.73 μg/mL, respectively. Enzyme inhibition was studied to investigate the effects of peonidin. The K values of peonidin were 114.33, 63.02, 2.99, 9.76, and 15.14 nM toward hCA I, hCA II, AChE, BChE, and α-glycosidase enzymes, respectively. Furthermore, peonidin's interactions with target enzymes BChE, hCA I, hCA II, AChE, and α-glycosidase were investigated by molecular docking. The results suggest that antioxidant-rich peonidin is a plant-based compound with potential use in the treatment of glaucoma, Alzheimer's disease, and diabetes. - Source: PubMed
Publication date: 2026/08/21
Karageçili HasanYerlikaya EmrahErtürk AdemAslan KübraAkıncıoglu HülyaGülçin İlhami - Alzheimer's disease (AD) is a progressive, multifactorial neurodegenerative condition characterized by neurofibrillary tangles, neuronal loss, cognitive impairment, and accumulation of β-amyloid plaques. Considering the limitations of current treatments, which present adverse effects and only alleviate symptoms without modifying disease progression, there is an urgent need for new therapeutic approaches. This study aimed to investigate the neuroprotective potential of synthetic derivatives of (1,4)-1,5-bis[(het)aryl]penta-1,4-dien-3-ones, focusing on the inhibition of the cholinesterase enzymes acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), targets directly related to the cholinergic deficit observed in AD. The compounds were initially synthesized by aldol condensation reactions, with subsequent physicochemical characterization. They were then subjected to in silico assays that demonstrated high binding affinity to the active sites of AChE and BChE. The derivatives were evaluated in vitro for their inhibitory activity on these enzymes and in vivo in an experimental model of AD induced by streptozotocin in Wistar rats. The synthesized derivatives showed favorable predicted interactions with the active sites of AChE and BChE, supporting their potential as cholinesterase inhibitors. In vitro assays demonstrated inhibitory activity against both enzymes, with selected derivatives showing improved activity compared with the parent scaffold. In the in vivo model, treatment with the selected compounds was associated with neuroprotective effects, suggesting preservation of nervous tissue integrity under AD-like conditions. These findings indicate that derivatives may represent promising candidates for further investigation as multitarget agents for AD. The study reinforces the relevance of integrating organic synthesis, molecular modeling, enzymatic assays, and in vivo evaluation in the search for new therapeutic strategies for neurodegenerative diseases. - Source: PubMed
Publication date: 2026/08/01
Mendes Géssica OliveiraBento Lucas Diego PereiraOliveira Thiago Malverde deBarbosa Deyse BritoTsui Guilherme SaraivaGomes Ellen NunesSales Raphaela OliveiraRocha Mateus Silva de CastroSilva Michel Pires daOliveira Tiago Alves deMaia Eduardo Habib BechelaneFalkoski Daniel LucianoMarra Isabella Flores de SouzaAndrade Lorena Silva MatosMendes Liliane Costa Vanessa PereiraFonseca Bianca de SouzaOliveira Lucas Matheus Gonçalves deSilva Victor Diogenes Amaral daCarvalho Paulo Batista deSilva Alisson Marques daTaranto Alex GutterresDamázio Laila Cristina MoreiraValle Marcelo SiqueiraLeite Franco Henrique Andrade - Investigating alternatives to synthetic chemicals in pest management is essential. The bioactivity of and essential oils (EOs) was evaluated against two stored-product insect pests ( and ) and two root-knot nematodes ( and ). EOs were hydrodistilled and analyzed by GC-MS: consisted mainly of myrtenyl acetate (47.10%) and β-thujone (11.41%); of methyleugenol (26.02%), β-asarone (14.04%), and elemicin (10.95%). In contact bioassays, caused 93.2-96.8% mortality against , but minimal effect on . caused 66.3-73.5% mortality against , no effect on , yet reduced progeny by 87%. Both EOs strongly repelled but weakly affected . exhibited 100% nematicidal efficacy against and 94.9% against ; showed limited effect. showed minimal hatching inhibition (<30%), whereas increased hatching. Sparse Partial Least Squares (sPLS) prioritized pulegone, methyleugenol, β-asarone, β-thujone, myrtenyl acetate, and β-phellandrene as constituents co-varying with AChE/BChE responses, with docking identifying pulegone as the top ligand. These findings demonstrate species-specific bioactivity patterns: shows strong nematicidal and reproductive inhibitory effects, whereas shows potent acute toxicity and repellency against , supporting multi-target biopesticide strategies to mitigate risks of synthetic chemical treatments. - Source: PubMed
Publication date: 2026/08/12
Evlice EmreAlkan MustafaKarakoç Ömer CemErtürk SaitBahtiyarca ReyhanYücel Yasemin YücelTüfekçi Ali RızaYırtıcı Ümit - Two novel axially substituted silicon phthalocyanines bearing 5,7-dichloro-8-hydroxy-2-methylquinoline (1a) and N-(hydroxymethyl)phthalimide (2a) moieties were synthesized and characterized by UV-Vis, FT-IR, H NMR, and mass spectrometry techniques. The biological potential of the synthesized compounds was evaluated through in vitro inhibition studies against acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and human carbonic anhydrase isoenzymes I and II (hCA I and hCA II). IC values were determined as 91.28 ± 25.21, 43.31 ± 20.35, 8.50 ± 2.80 and 23.35 ± 12.98 µM, for compound 1a, and 2.78 ± 1.05, 4.88 ± 1.50, 0.94 ± 1.06 and 4.15 ± 3.01 µM for compound 2a against AChE, BChE, hCA I, and hCA II enzymes respectively. Compound 2a exhibited remarkable inhibitory activity. Molecular docking results supported the experimental findings, indicating that compound 2a exhibited significantly higher inhibitory potency than compound 1a. Structure-activity relationship analysis demonstrated that compound 2a exhibits improved enzyme inhibition. The combined experimental and computational findings showed that compound 2a is a promising multifunctional enzyme inhibitor. Compound 2a exhibited remarkable inhibitory activity across all targets. Molecular docking supported the experimental findings, with compound 2a showing more favorable Vinardo binding affinities (-8.11, -3.94, -7.39, and -7.15 kcal/mol against AChE, BChE, hCA I, and hCA II, respectively) than compound 1a, primarily through additional hydrogen-bonding interactions provided by its phthalimide groups. The docking protocol was validated by redocking the co-crystallized ligands, which reproduced the crystallographic poses with RMSD values below 2.0 Å for all targets. DFT calculations revealed narrow HOMO-LUMO energy gaps (0.666 eV for 1a and 0.881 eV for 2a), consistent with the high reactivity of the phthalocyanine core, while in silico ADMET analysis indicated favorable toxicity profiles for both compounds. The combined experimental and computational findings identify compound 2a as a promising multifunctional enzyme inhibitor. - Source: PubMed
Ünlü SedaKöksal ZeynepKırboğa Kevser KübraTuncel Elmalı Fikriye - To determine whether butyrylcholinesterase (BChE) activity independently predicts in-hospital mortality in critically ill adults and to derive a prognostic threshold from patient-level data. - Source: PubMed
Publication date: 2026/08/25
Esper Treml RicardoGrillo Iago T CHrabovska AnnaFazekas TomasEspeter FlorianSchmidt KarstenCaldonazo TulioPassos Felipe SGessolo Lins Paulo RicardoDimidega ThaisEhler JohannesBasile Filho AnibalDecker Sebastian OZivkovic Aleksandar Rda Silva Joao Manoel