Interaction of Thalassia testudinum Metabolites with Cytochrome P450 Enzymes and Its Effects on Benzo(a)pyrene-Induced Mutagenicity

Delgado-Roche, Liván; Santes-Palacios, Rebeca; Herrera, J.; Hernández, Santiago Cortés; Riera, Mario; Fernández, Miguel D.; Mesta, Fernando; Garrido, Gabino; Rodeiro, Idania; Espinosa-Aguirre, J.J.

doi:10.3390/md18110566

Cited by 7 publications

(1 citation statement)

References 65 publications

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“…Similar behavior was observed by Shields et al [ 31 ] with quassinoids and by Delgado-Roche et al [ 36 ] with a hydroethanolic extract of the seagrass Thalassia testudinum (Hydrocharitaceae). These authors associated this behavior with the difference between amino acid residues within each active site.…”

Section: Resultssupporting

confidence: 85%

Inhibition of the CYP Enzymatic System Responsible of Heterocyclic Amines Bioactivation by an Asclepias subulata Extract

Gutiérrez-Pacheco

Peña‐Ramos

Santes-Palacios

et al. 2023

Plants

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Asclepias subulata plant extract has previously demonstrated antiproliferative activity and antimutagenicity against heterocyclic aromatic amines (HAAs) commonly found in cooked meat. The objective of this work was to evaluate the in vitro ability of an ethanolic extract from the medicinal plant Asclepias subulata extract (ASE), non-heated and heated (180 °C), to inhibit the activity of CYP1A1 and CYP1A2, which are largely responsible for HAAs bioactivation. Ethoxyresorufin and methoxyresorufin O-dealkylation assays were performed in rat liver microsomes exposed to ASE (0.002–960 µg/mL). ASE exerted an inhibitory effect in a dose-dependent manner. The half inhibitory concentration (IC50) for unheated ASE was 353.6 µg/mL and 75.9 µg/mL for heated ASE in EROD assay. An IC40 value of 288.4 ± 5.8 µg/mL was calculated for non-heated ASE in MROD assay. However, after heat treatment, the IC50 value was 232.1 ± 7.4 µg/mL. Molecular docking of corotoxigenin-3-O-glucopyranoside, one of the main components of ASE, with CYP1A1/2 structure, was performed. Results show that the interaction of corotoxigenin-3-O-glucopyranoside with CYP1A1/2s’ α-helices, which are related with the active site and the heme cofactor, may explain the plant extract’s inhibitory properties. Results showed that ASE inhibits CYP1A enzymatic subfamily and may potentially act as a chemopreventive agent by inhibiting bioactivation of promutagenic dietary HAAs.

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Section: Resultssupporting

confidence: 85%