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. 2020 Sep 8;9(9):840.
doi: 10.3390/antiox9090840.

Effects of Moringa oleifera Leaf Extract on Diabetes-Induced Alterations in Paraoxonase 1 and Catalase in Rats Analyzed through Progress Kinetic and Blind Docking

Erick Sierra-Campos  1 , Mónica Valdez-Solana  1 , Claudia Avitia-Domínguez  2 , Mara Campos-Almazán  2 , Ismael Flores-Molina  1 , Guadalupe García-Arenas  3 , Alfredo Téllez-Valencia  2
Affiliations

Effects of Moringa oleifera Leaf Extract on Diabetes-Induced Alterations in Paraoxonase 1 and Catalase in Rats Analyzed through Progress Kinetic and Blind Docking

Erick Sierra-Campos et al. Antioxidants (Basel). .

Abstract

In our study, we aimed to evaluate the effects of Moringa oleifera leaves extract on rat paraoxonase 1 (rPON1) and catalase (rCAT) activities in alloxan-induced diabetic rats. Our study included three groups; group C (control, n = 5); group D (diabetic, n = 5); and group DM (M. oleifera extract-supplemented diabetic rats, n = 5). Daily oral administration of M. oleifera extract at 200 mg/kg doses produced an increase in endogenous antioxidants. Serum rPON1 (lactonase) and liver cytosol catalase activities were determined by a spectrophotometric assay using progress curve analysis. We found a decrease in the Vm value of rPON1 in diabetic rats, but dihydrocoumarin (DHC) affinity (Km) was slightly increased. The value of Vm for the DM group was found to be reduced approximately by a factor of 3 compared with those obtained for group C, whereas Km was largely changed (96 times). Catalase activity was significantly higher in the DM group. These data suggest that the activation of rPON1 and rCAT activities by M. oleifera extracts may be mediated via the effect of the specific flavonoids on the enzyme structure. In addition, through molecular blind docking analysis, rPON1 was found to have two binding sites for flavonoids. In contrast, flavonoids bound at four sites in rCAT. In conclusion, the data suggest that compounds from M. oleifera leaves extract were able to influence the catalytic activities of both enzymes to compensate for the changes provoked by diabetes in rats.

Keywords: Moringa oleifera leaves extract; progress kinetics and blind docking; rat liver catalase; serum paraoxonase 1.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Calculation of Km and Vm from substrate concentration versus time plots. The image shows a representative trace of five repetitions for each rat of a different group.
Figure 2
Figure 2
Calculation of Km and Vm from substrate concentration versus time plots. The image shows a representative trace of five repetitions for each rat of a different group.
Figure 3
Figure 3
Binding of all compounds in (A) rPON1 and (B) rCAT in bind docking protocol.
Figure 4
Figure 4
Binding mode of compound (A) 49 and (C) 26 in rPON1, as well as 2D interaction map for (B) 49 and (D) 26.
Figure 5
Figure 5
Binding mode of compound (A) 15, (C) 16, (E) 4, and (G) 43 in rat liver catalase monomer, as well as 2D interaction map for (B) 15, (D) 16, (F) 4, and (H) 43.
Figure 5
Figure 5
Binding mode of compound (A) 15, (C) 16, (E) 4, and (G) 43 in rat liver catalase monomer, as well as 2D interaction map for (B) 15, (D) 16, (F) 4, and (H) 43.
See this image and copyright information in PMC

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