Fidyasari, Ambar and Estiasih, Teti and Khatib, Alfi and Wulan, Siti Narsito and Raharjo, Sentot Joko
(2025)
Molecular dynamics simulation of bioactive compounds from Moringa oleifera leaf powder extract as antidiabetic by inhibiting α-amylase and α-glucosidase enzymes.
Trends in Sciences, 23 (1).
pp. 1-18.
E-ISSN 2774-0226
Abstract
Diabetes is a chronic disease that has caused around 6.7 million deaths a year or one death every 5 s. Diabetes therapy usually focuses on the insulin hormone. In fact, in addition to regulating carbohydrate metabolism by the insulin hormone, therapy can be done by inhibiting several enzymes such as α-amylase and α-glucosidase in the starch and glycogen metabolism pathway as a source of blood glucose. This study investigates Moringa oleifera leaf powder (MOLP) from different Leaf stalk colors were screened for their inhibitory action of α-amylase and α-glucosidase against type 2 diabetes through molecular docking, molecular dynamics simulation, and in vitro enzyme inhibition. Rutin showed the highest binding affinity among 57 tested compounds. This compound simultaneously binds to the 2 target proteins of α-amylase and α-glucosidase, with higher binding affinity values of –6.752 mol–1 for α-amylase and –8.756 mol–1 for α-glucosidase. The rutin glucosidase revealed to be the most stable molecule with the highest binding free energy through molecular dynamics simulation was MM-GBSA Binding Energy = –33.3645 ± 5.0338 kcal mol–1 and MM-PBSA Binding Energy = 1.8598 ± 5.5359 kcal mol–1, indicating that it could compete with the inhibitor native ligand. The α-glucosidase inhibitory activity of the ethyl acetate extract achieved 81.58% inhibition, while acarbose achieved 84.47%. Rutin has the best potential as an inhibitor of the α-glucosidase enzyme and the stability of its interaction compared to other flavonoid groups, making it a prospective drug candidate for type 2 diabetes
Actions (login required)
 |
View Item |
Download Statistics
Download Statistics