ArticleBiophysical journal2005
Influence of the water structure on the acetylcholinesterase efficiency.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Structural Bioinformatics Applied to Acetylcholinesterase Enzyme Inhibition.International journal of molecular sciences · 2025Review
- Fluorescence Spectroscopy Shows Porphyrins Produced by Cultured Oral Bacteria Differ Depending on Composition of Growth Media.Caries research · 2023Article
- Erythrocyte acetylcholinesterase as biomarker of pesticide exposure: new and forgotten insights.Environmental science and pollution research international · 2018Review
- Binding free energy calculations to rationalize the interactions of huprines with acetylcholinesterase.Journal of computer-aided molecular design · 2018Article
- X-ray scattering experiments with high-flux X-ray source coupled rapid mixing microchannel device and their potential for high-flux neutron scattering investigations.The European physical journal. E, Soft matter · 2013Article
- Preparation and Characterization of Porous Gold and its Application as a Platform for Immobilization of Acetylcholine Esterase.Chemistry of materials : a publication of the American Chemical SocietyArticle
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Authors and funding
2 authors.
Funding
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Abstract
We have studied the catalytic efficiency of acetylcholinesterase (AChE) in various solutions with ion-disturbed water structure to explore the role that the water structure plays in the substrate-enzyme encounter. The extent of water structuring in the different aqueous solutions was determined by near-infrared spectroscopy. The influence of water structure on the degree of solvation and on the intramolecular mobility of AChE was investigated for different aqueous ionic solutions by small-angle x-ray scattering technique and depolarization fluorescence spectroscopy. It was found that the encounter process between AChE and acetylthiocholine was promoted in solutions with less structured water. In these solutions it was also found that AChE is less solvated coinciding with higher intramolecular mobility. The found experimental results suggest that the water structure may influence the substrate-enzyme encounter process by diminishing the AChE solvation shell and may help diffusion of the substrate through the gorge by enhancing the intramolecular mobility of AChE.
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