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Title

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

 

Authors

Dyah Ratna Wulan1, 2, Edi Priyo Utomo3* & Chanif Mahdi3

 

Affiliation

1Master Program of Chemistry, Faculty of Science, Brawijaya University; 2Academy of Food and Pharmacy Analyst, Putra Indonesia Malang; 3Chemistry Department, Faculty of Science, Brawijaya University, Malang, Indonesia

 

Email

edipu2000@yahoo.com; *Corresponding author

 

Article Type

Hypothesis

 

Date

Received March 21, 2014; Accepted April 03, 2014; Published April 23, 2014

 

Abstract

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-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- 39460ÁM in rat and 0.67-5600ÁM 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 (0.67ÁM) than acarbose (2.6 ÁM), which suggesting that betulin is more potential as inhibitor than acarbose, but this assumption must be verified in vitro.

 

Keywords

alpha amylase inhibitor, betulin, docking, Ruellia tuberosa L

 

Citation

Wulan et al. Bioinformation 10(4): 209-215 (2014)

 

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.