In:
Natural Resources for Human Health, Visagaa Publishing House, Vol. 2, No. 2 ( 2022-1-16), p. 265-273
Abstract:
Diabetes mellitus is a major public health problem in the world. In Africa, more than 80% of patients use plants for their treatment. However, the methods of validation of endogenous knowledge usually used are costly. The alternative method developed in this study aims at creating hyperglycemia 〈 i 〉 in vitro 〈 /i 〉 and exploiting the metabolic pathway involving glucose oxidase for UV-visible spectrophotometric screening of medicinal plants’ antidiabetic activity. The evolution of glucose oxidation as a function of drug concentration is followed by UV-visible spectrophotometry. The formation of the stable complex between the enzyme and the inhibitor is studied using molecular docking. Drugs used (Gliben) and plant extracts exhibited an 〈 i 〉 in vitro 〈 /i 〉 hypoglycemic effect by reducing exponentially, 〈 i 〉 in vitro 〈 /i 〉 , the level of free glucose. The results also showed that 〈 i 〉 L. multiflora 〈 /i 〉 is more active than 〈 i 〉 V. amygdalina 〈 /i 〉 (IC 〈 sub 〉 50 〈 /sub 〉 : 1.36 ± 0.09 mg/mL Vs IC 〈 sub 〉 50 〈 /sub 〉 : 3.00 ± 0.54 mg/mL). Gliben (0.5 mg/mL) and 〈 i 〉 L. multiflora 〈 /i 〉 (2 mg/mL) reduced both the rate of oxidation of glucose by glucose oxidase (catalytic power V 〈 sub 〉 max 〈 /sub 〉 : 0.84 ± 0.11 mg*mL 〈 sup 〉 -1 〈 /sup 〉 *min 〈 sup 〉 -1 〈 /sup 〉 for Gliben and 1.72 ± 0.13 mg*mL 〈 sup 〉 -1 〈 /sup 〉 *min 〈 sup 〉 -1 〈 /sup 〉 for 〈 sup 〉 L. multiflora 〈 /sup 〉 ); and the affinity of this enzyme for its substrate-glucose (K 〈 sub 〉 M 〈 /sub 〉 : 15.11 ± 2.72 mg*mL 〈 sup 〉 -1 〈 /sup 〉 for Gliben and 9.17 ± 1.56 mg*mL 〈 sup 〉 -1 〈 /sup 〉 for 〈 i 〉 L. multiflora 〈 /i 〉 ) when these results are compared to enzyme catalysis in the absence of inhibitor (V 〈 sub 〉 max 〈 /sub 〉 : 2.86 ± 0.44 mg*mL 〈 sup 〉 -1 〈 /sup 〉 *min-1; K 〈 sub 〉 M 〈 /sub 〉 : 8.07 ± 1.96 mg*mL 〈 sup 〉 -1 〈 /sup 〉 ). The binding of GOX (1GAL) to selected phytocompounds derived from 〈 i 〉 L. multiflora 〈 /i 〉 was confirmed by molecular docking. The most stable complexes were obtained for four compounds; 〈 b 〉 8 〈 /b 〉 (-10.1±0.0 Kcal/mol), 〈 b 〉 6 〈 /b 〉 (-9.5±0.1 Kcal/mol), 〈 b 〉 3 〈 /b 〉 (-8.3±0.0 Kcal/mol) and 〈 b 〉 9 〈 /b 〉 (-8.2±0.1 Kcal/mol). Among these, compounds 〈 b 〉 8 〈 /b 〉 and 〈 b 〉 6 〈 /b 〉 formed complexes with the enzyme stabilized by hydrogen bonds, the compound 〈 b 〉 8 〈 /b 〉 forms 5 hydrogen bonds ( 〈 b 〉 ASN514 〈 /b 〉 , 〈 b 〉 ASP424 〈 /b 〉 , 〈 b 〉 ARG95 〈 /b 〉 , 〈 b 〉 TYP68 〈 /b 〉 , 〈 b 〉 LEU65 〈 /b 〉 ) while compound 〈 b 〉 6 〈 /b 〉 forms 2 hydrogen bonds ( 〈 b 〉 ASN514 〈 /b 〉 and 〈 b 〉 SER422 〈 /b 〉 ). However, no H-bonding interaction occurs in the complex that involves ligands 〈 b 〉 9 〈 /b 〉 and 〈 b 〉 3 〈 /b 〉 despite their high binding energy (-8.2±0.1 Kcal/mol and -8.3±0.0 Kcal/mol respectively). Glucose oxidase can serve as a marker enzyme for 〈 i 〉 in vitro 〈 /i 〉 antidiabetic activity evaluation of medicinal plants.
Type of Medium:
Online Resource
ISSN:
2583-1194
DOI:
10.53365/nrfhh/144779
Language:
Unknown
Publisher:
Visagaa Publishing House
Publication Date:
2022
