Title

Molecular docking analysis of phytoconstituent from Momordica charantia with Guanylate Cyclase catalytic domain

Authors

Mohankrishna Ghanta¹, Elango Panchanathan^1*, Bhaskar Venkata Kameswara Subrahmanya Lakkakula², Anbumani Narayanaswamy³, P.A.Abhinand⁴, Stalin Antony⁵

Affiliation

¹Department of Pharmacology, Sri Ramachandra Medical College and Research Institute- Deemed to be University, Chennai-600116, Tamil Nadu, India;

²Department of Molecular Genetics, Research Division, Sickle Cell Institute Chhattisgarh, Raipur- 492001, Chhattisgarh, India;

³Department of Microbiology, Sri Ramachandra Medical College and Research Institute- Deemed to be University, Chennai-600116, Tamil Nadu, India;

⁴Department of Bioinformatics, Sri Ramachandra Medical College and Research Institute- Deemed to be University, Chennai-600116, Tamil Nadu, India;

⁵Centre for Advanced Studies in Botany and Centre for Herbal Sciences, University of Madras, Guindy Campus, Chennai – 600 025, Tamil Nadu, India

Email

drpelango@yahoo.com

Article Type

Hypothesis

Date

Received July 7, 2018; Revised July 11, 2018; Accepted July 30, 2018; Published July 31, 2018

Soluble guanylate cyclase (sGC) is a type of lyase enzyme with profoundly increasing importance in treatments of cardiovascular and neurodegenerative disorders. Modulation of sGC activity demonstrated beneficial effects against Parkinson's disease by reducing glutamate excitotoxicity. It is of interest to evaluate the pharmacological activity of Momordica charantia phytoconstituent (DGalacturonic acid) and ODQ with catalytic domain of sGC enzyme, using Autodock version 4.2 programs. Docking results revealed the binding ability of ODQ at the allosteric sites of sGC. D-galacturonic acid also shows binding interaction at the same allosteric sites in the catalytic domain of sGC like ODQ. Results show that both the ligands have efficient binding to THR 474 amino acid residue of beta 1 subunit of the enzyme. The drug likeliness score further implies the suitability of D-Galacturonic acid as a drug-like molecule. The binding property of ODQ and D-Galacturonic acid with the catalytic domain help to inhibit sGC activity having pharmacological effects. Moreover, ODQ interaction with heme site of sGC is already known while its interaction with the catalytic domain is shown in this report.

Keywords

In silico screening, ODQ, soluble Guanylate cyclase

Citation

Ghanta et al. Bioinformation 14(7): 378-383 (2018)

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.