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

Autor:	Ghanta M; Department of Pharmacology, Sri Ramachandra Medical College and Research Institute- Deemed to be University, Chennai-600116, Tamil Nadu, India., Panchanathan E; Department of Pharmacology, Sri Ramachandra Medical College and Research Institute- Deemed to be University, Chennai-600116, Tamil Nadu, India., Lakkakula BVKS; Department of Molecular Genetics, Research Division, Sickle Cell Institute Chhattisgarh, Raipur- 492001, Chhattisgarh, India., Narayanaswamy A; Department of Microbiology, Sri Ramachandra Medical College and Research Institute- Deemed to be University, Chennai-600116, Tamil Nadu, India., Abhinand PA; Department of Bioinformatics, Sri Ramachandra Medical College and Research Institute- Deemed to be University, Chennai-600116, Tamil Nadu, India., Antony S; Centre for Advanced Studies in Botany and Centre for Herbal Sciences, University of Madras, Guindy Campus, Chennai-600 025, Tamil Nadu, India.
Jazyk:	angličtina
Zdroj:	Bioinformation [Bioinformation] 2018 Jul 31; Vol. 14 (7), pp. 378-383. Date of Electronic Publication: 2018 Jul 31 (Print Publication: 2018).
DOI:	10.6026/97320630014378
Abstrakt:	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.
Databáze:	MEDLINE
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