Related Experiment Video
Updated: May 14, 2025

Cell-free Biochemical Fluorometric Enzymatic Assay for High-throughput Measurement of Lipid Peroxidation in High Density Lipoprotein
Published on: October 12, 2017
Acetylcholinesterase Inhibition and Antioxidant Activity of DHA-Disubstituted Phospholipids
Ernestina Garcia-Quinto1, Sabrina Sollecito-Rovella1, Victor M Amador-Luna2
1Laboratory of Microbiology and Food Biocatalysis, Institute of Food Science Research (CIAL, CSIC-UAM), Madrid, Spain.
Abstract:
Docosahexaenoic acid (DHA) is an essential fatty acid for the central nervous system. It plays a crucial role in brain health and the prevention of neurodegenerative diseases, particularly in its phospholipid form, which has greater bioavailability. Previous studies, conducted by our group, enabled the enzymatic synthesis of pure disubstituted DHA phospholipids (1,2-Di-DHA-PC). In the present study, the inhibitory activities of 1,2-Di-DHA-PC on acetylcholinesterase (AChE) and its antioxidant capacity were evaluated. The results showed that 1,2-Di-DHA-PC exhibited significant inhibition of the AChE enzyme. Moreover, 1,2-Di-DHA-PC showed antioxidant capacity compared to ascorbic acid, a natural antioxidant par excellence. These findings highlight the therapeutic potential of 1,2-Di-DHA-PC in the treatment of neurodegenerative diseases and its ability to offer protection against the lipid peroxidation of the neuronal aging process, one of the main drivers of neurodegeneration, suggesting the need for further studies to confirm its clinical applicability.
More Related Videos
08:20Investigating the Protective Effects of Platycodin D on Non-Alcoholic Fatty Liver Disease in a Palmitic Acid-Induced In Vitro Model
Published on: December 2, 2022
13:05Enzymatic Synthesis of Epoxidized Metabolites of Docosahexaenoic, Eicosapentaenoic, and Arachidonic Acids
Published on: June 28, 2019
Related Concept Videos
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex,...
Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...
Anticholinesterase Agents: Poisoning and Treatment
Irreversible agents form a strong bond with the cholinesterase enzyme, making it inactive. The breakdown of the phosphorylated enzyme is...
Indirect-Acting Cholinergic Agonists: Pharmacological Actions
At the neuromuscular junction, these agents work by inhibiting the breakdown of acetylcholine, allowing it to remain bound to the receptor and bind to nearby receptors. This process leads to repetitive firing of the endplate, causing muscle...
Direct-Acting Cholinergic Agonists: Pharmacokinetics
Indirect-Acting Cholinergic Agonists: Pharmacokinetics
Reversible agents containing quaternary amines, such as neostigmine and edrophonium, are not easily absorbed orally because they...