Dataset Information

Molecular modeling of Ruellia tuberosa L compounds as a-amylase inhibitor: an in silico comparation between human and rat enzyme model.

ABSTRACT: Inhibition of ?-amylase is an important strategy to control post-prandial hyperglycemia. The present study on Ruellia tuberosa, known as traditional anti-diabetic agent, is being provided in silico study to identify compounds inhibiting ?-amylase in rat and human. Compounds were explored from PubChem database. Molecular docking was studied using the autodock4. The interactions were further visualized and analyzed using the Accelrys Discovery Studio version 3.5. Binding energy of compounds to ?-amylase was varying between -1.92 to -6.66 kcal/mol in rat pancreatic alpha amylase and -3.06 to -8.42kcal/mol in human pancreatic alpha amylase, and inhibition konstanta (ki) was varying between 13.12- 39460µM in rat and 0.67-5600µM in human. The docking results verify that betulin is the most potential inhibitor of all towards rat model alpha amylase and human alpha amylase. Further analysis reveals that betulin could be a potential inhibitor with non-competitive pattern like betulinic acid. In comparison, betulin has smaller Ki (0.67µM) than acarbose (2.6 µM), which suggesting that betulin is more potential as inhibitor than acarbose, but this assumption must be verified in vitro.

SUBMITTER: Wulan DR

PROVIDER: S-EPMC4070051 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Molecular modeling of Ruellia tuberosa L compounds as a-amylase inhibitor: an in silico comparation between human and rat enzyme model.

Wulan Dyah Ratna DR Utomo Edi Priyo EP Mahdi Chanif C

Bioinformation 20140423 4

Inhibition of α-amylase is an important strategy to control post-prandial hyperglycemia. The present study on Ruellia tuberosa, known as traditional anti-diabetic agent, is being provided in silico study to identify compounds inhibiting α-amylase in rat and human. Compounds were explored from PubChem database. Molecular docking was studied using the autodock4. The interactions were further visualized and analyzed using the Accelrys Discovery Studio version 3.5. Binding energy of compounds to α-a ...[more]

PMID: 24966522

Similar Datasets

Project description:Diabetes is a chronic metabolic disorder characterized by raised glucose levels in the blood, resulting in grave damage over time to various body organs, including the nerves, heart, kidneys, eyes, and blood vessels. One of its therapeutic treatment approaches involves the inhibition of enzymes accountable for carbohydrate digestion and absorption. The present work is aimed at evaluating the potential of some reported metabolites from Garcinia mangostana (mangosteen, Guttiferae) as alpha-amylase inhibitors. Forty compounds were assessed for their capacity to inhibit alpha-amylase using in silico studies as well as in vitro assays. Molecular docking was carried out to analyze their binding capacities in the 3D structure of alpha-amylase (PDB ID: 4GQR). Among the tested compounds, 6-O-β-D-glucopyranosyl-2,4,6,3',4',6'-hexahydroxybenzophenone (8), aromadendrin-8-C-glucoside (5), epicatechin (6), rhodanthenone (4), and garcixanthone D (40) had a high XP G.score and a Glide G.score of -12.425, -11.855, -11.135, and -11.048 Kcal/mol, respectively. Compound 8 possessed the XP and Glide docking score of -12.425 Kcal/mol compared to the reference compounds myricetin and acarbose which had an XP and Glide docking score of -12.319 and 11.201 Kcal/mol, respectively. It interacted through hydrogen bond formations between its hydroxyl groups and the residues His 101, Asp 197, Glu 233, Asp 300, and His 305, in addition to water bridges and hydrophobic interactions. Molecular mechanics-generalized born surface area (MM-GBSA) was used to calculate the binding free energy and molecular dynamic studies that indicated the stability of the alpha-amylase-compound 8 complex during the 100 ns simulation in comparison with myricetin- and acarbose-alpha-amylase complexes. Additionally, the in vitro alpha-amylase inhibition assay findings validated the in silico study's findings. This could further validate the potential of G. mangostana as a candidate for diabetes management.

Dataset Information

Molecular modeling of Ruellia tuberosa L compounds as a-amylase inhibitor: an in silico comparation between human and rat enzyme model.

Publications

Molecular modeling of Ruellia tuberosa L compounds as a-amylase inhibitor: an in silico comparation between human and rat enzyme model.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets