Inactivation of lipoxygenase and cyclooxygenase by natural betalains and semi-synthetic analogues
| Autor: | José Manuel López-Nicolás, Fernando Gandia-Herrero, Pedro Jesús Vidal, José manuel López nicolás, Francisco Garcia-Carmona |
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| Rok vydání: | 2014 |
| Předmět: |
Stereochemistry
Lipoxygenase Betalains Analytical Chemistry Enzyme catalysis chemistry.chemical_compound Betalain Humans Cyclooxygenase Inhibitors Lipoxygenase Inhibitors chemistry.chemical_classification Molecular Structure biology Plant Extracts Active site Biological activity General Medicine Enzyme Activation Molecular Docking Simulation Kinetics Enzyme Biochemistry chemistry Prostaglandin-Endoperoxide Synthases Docking (molecular) biology.protein Cyclooxygenase Beta vulgaris Food Science |
| Zdroj: | Food Chemistry. 154:246-254 |
| ISSN: | 0308-8146 |
| DOI: | 10.1016/j.foodchem.2014.01.014 |
| Popis: | Betalains are natural pigments characteristic of plants of the order Caryophyllales. In this work, the role of betalains in the anti-inflammatory activity described for plant extracts is analysed in terms of the inactivation of the enzymes involved in the biochemical response (lipoxygenase and cyclooxygenase). Pure natural betalains and semi-synthetic analogues are demonstrated to promote a significant reduction of the enzymes activity. Reactions were followed spectrophotometrically and by HPLC-DAD. Phenethylamine-betaxanthin was the most potent in the inactivation of cyclooxygenase, with a reduction of 32% of the control activity at 125μM, while the natural pigment betanidin and a betalain analogue derived from indoline resulted as the most potent inactivators of lipoxygenase, with IC50 values of 41.4 and 40.1μM, respectively. Molecular docking studies revealed that betalains interact with the lipoxygenase amino acids involved in substrate binding and with Tyr-385 and Ser-530 close to the cyclooxygenase active site, interfering in enzyme catalysis. |
| Databáze: | OpenAIRE |
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