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The red seaweed Laurencia viridis is a rich source of oxygenated secondary metabolites that were derived from squalene. We report here the structures of three novel compounds, (+)-longilene peroxide (1), longilene (2), and (+)-prelongilene (3) that were isolated from this alga, in addition to other substances, 4 and 5, resulting from their acid-mediated degradation. The effect of compounds 1 and 3 against Ser-Thr protein phosphatase type 2A (PP2A) was evaluated, showing that (+)-longilene peroxide (1) inhibited PP2A (IC50 11.3 μM). In order to explain the interaction between PP2A and compounds 1 and 3, molecular docking simulations onto the PP2A enzyme-binding region were used.
Squalene, Aquatic Organisms, QH301-705.5, Phosphatase inhibition, Laurencia viridis, Marine polyether, Laurencia, Article, Structure-Activity Relationship, docking simulation, Protein Phosphatase 2, Biology (General), Enzyme Inhibitors, red alga, Red alga, Biological Products, longilenes, Seaweed, marine polyether, phosphatase inhibition, Molecular Docking Simulation, Docking simulation, phosphatase inhibition; marine polyether; longilenes; docking simulation; red alga; <i>Laurencia viridis</i>, Protein Binding
Squalene, Aquatic Organisms, QH301-705.5, Phosphatase inhibition, Laurencia viridis, Marine polyether, Laurencia, Article, Structure-Activity Relationship, docking simulation, Protein Phosphatase 2, Biology (General), Enzyme Inhibitors, red alga, Red alga, Biological Products, longilenes, Seaweed, marine polyether, phosphatase inhibition, Molecular Docking Simulation, Docking simulation, phosphatase inhibition; marine polyether; longilenes; docking simulation; red alga; <i>Laurencia viridis</i>, Protein Binding
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