Molecular docking analysis of phytic acid and 4-hydroxyisoleucine as cyclooxygenase-2, microsomal prostaglandin e synthase-2, tyrosinase, human neutrophil elastase, matrix metalloproteinase-2 and -9, xanthine oxidase, squalene synthase, nitric oxide synthase, human aldose reductase, and lipoxygenase inhibitors

Radhakrishnan Narayanaswamy, Kok Wai Lam, Norhaizan Esa

Research output: Contribution to journalArticle

Abstract

Background: The phytoconstituents phytic acid and 4-hydroxyisoleucine have been reported to posses various biological properties. Objective: This prompted us to carry out the docking study on these two ligands (phytic acid & 4-hydroxyisoleucine) against eleven targeted enzymes. Materials and Methods: Phytic acid & 4-hydroxyisoleucine were evaluated on the docking behaviour of cyclooxygenase-2 (COX-2), microsomal prostaglandin E synthase-2 (mPGES-2), tyrosinase, human neutrophil elastase (HNE), matrix metalloproteinase (MMP 2 and 9), xanthine oxidase (XO), squalene synthase (SQS), nitric oxide synthase (NOS), human aldose reductase (HAR) and lipoxygenase (LOX) using Discovery Studio Version 3.1 (except for LOX, where Autodock 4.2 tool was used). Results: Docking and binding free energy analysis revealed that phytic acid exhibited the maximum binding energy for four target enzymes such as COX-2, mPGES-2, tyrosinase and HNE. Interestingly, we found that 4-hydroxyisoleucine has the potential to dock and bind with all of the eleven targeted enzymes. Conclusion: This present study has paved a new insight in understanding 4-hydroxyisoleucine as potential inhibitor against COX-2, mPGES-2, tyrosinase, HNE, MMP 2, MMP 9, XO, SQS, NOS, HAR and LOX.

Original languageEnglish
Pages (from-to)S512-S518
JournalPharmacognosy Magazine
Volume13
Issue number51
DOIs
Publication statusPublished - 2017

Fingerprint

Farnesyl-Diphosphate Farnesyltransferase
Molecular Docking Simulation
Lipoxygenase Inhibitors
Aldehyde Reductase
Leukocyte Elastase
Phytic Acid
Monophenol Monooxygenase
Xanthine Oxidase
Matrix Metalloproteinase 2
Matrix Metalloproteinase 9
Cyclooxygenase 2
Prostaglandin-Endoperoxide Synthases
Nitric Oxide Synthase
Lipoxygenase
Matrix Metalloproteinases
Enzymes
Cyclooxygenase 2 Inhibitors
4-hydroxyisoleucine
Ligands
Prostaglandin-E Synthases

Keywords

  • 4-hydroxyisoleucine
  • cyclooxygenase-2
  • microsomal prostaglandin E synthase-2
  • molecular docking
  • phytic acid
  • tyrosinase

ASJC Scopus subject areas

  • Pharmaceutical Science
  • Drug Discovery

Cite this

@article{64485a92de4b418da2034875f40065e2,
title = "Molecular docking analysis of phytic acid and 4-hydroxyisoleucine as cyclooxygenase-2, microsomal prostaglandin e synthase-2, tyrosinase, human neutrophil elastase, matrix metalloproteinase-2 and -9, xanthine oxidase, squalene synthase, nitric oxide synthase, human aldose reductase, and lipoxygenase inhibitors",
abstract = "Background: The phytoconstituents phytic acid and 4-hydroxyisoleucine have been reported to posses various biological properties. Objective: This prompted us to carry out the docking study on these two ligands (phytic acid & 4-hydroxyisoleucine) against eleven targeted enzymes. Materials and Methods: Phytic acid & 4-hydroxyisoleucine were evaluated on the docking behaviour of cyclooxygenase-2 (COX-2), microsomal prostaglandin E synthase-2 (mPGES-2), tyrosinase, human neutrophil elastase (HNE), matrix metalloproteinase (MMP 2 and 9), xanthine oxidase (XO), squalene synthase (SQS), nitric oxide synthase (NOS), human aldose reductase (HAR) and lipoxygenase (LOX) using Discovery Studio Version 3.1 (except for LOX, where Autodock 4.2 tool was used). Results: Docking and binding free energy analysis revealed that phytic acid exhibited the maximum binding energy for four target enzymes such as COX-2, mPGES-2, tyrosinase and HNE. Interestingly, we found that 4-hydroxyisoleucine has the potential to dock and bind with all of the eleven targeted enzymes. Conclusion: This present study has paved a new insight in understanding 4-hydroxyisoleucine as potential inhibitor against COX-2, mPGES-2, tyrosinase, HNE, MMP 2, MMP 9, XO, SQS, NOS, HAR and LOX.",
keywords = "4-hydroxyisoleucine, cyclooxygenase-2, microsomal prostaglandin E synthase-2, molecular docking, phytic acid, tyrosinase",
author = "Radhakrishnan Narayanaswamy and Lam, {Kok Wai} and Norhaizan Esa",
year = "2017",
doi = "10.4103/pm.pm_195_16",
language = "English",
volume = "13",
pages = "S512--S518",
journal = "Pharmacognosy Magazine",
issn = "0973-1296",
publisher = "Medknow Publications and Media Pvt. Ltd",
number = "51",

}

TY - JOUR

T1 - Molecular docking analysis of phytic acid and 4-hydroxyisoleucine as cyclooxygenase-2, microsomal prostaglandin e synthase-2, tyrosinase, human neutrophil elastase, matrix metalloproteinase-2 and -9, xanthine oxidase, squalene synthase, nitric oxide synthase, human aldose reductase, and lipoxygenase inhibitors

AU - Narayanaswamy, Radhakrishnan

AU - Lam, Kok Wai

AU - Esa, Norhaizan

PY - 2017

Y1 - 2017

N2 - Background: The phytoconstituents phytic acid and 4-hydroxyisoleucine have been reported to posses various biological properties. Objective: This prompted us to carry out the docking study on these two ligands (phytic acid & 4-hydroxyisoleucine) against eleven targeted enzymes. Materials and Methods: Phytic acid & 4-hydroxyisoleucine were evaluated on the docking behaviour of cyclooxygenase-2 (COX-2), microsomal prostaglandin E synthase-2 (mPGES-2), tyrosinase, human neutrophil elastase (HNE), matrix metalloproteinase (MMP 2 and 9), xanthine oxidase (XO), squalene synthase (SQS), nitric oxide synthase (NOS), human aldose reductase (HAR) and lipoxygenase (LOX) using Discovery Studio Version 3.1 (except for LOX, where Autodock 4.2 tool was used). Results: Docking and binding free energy analysis revealed that phytic acid exhibited the maximum binding energy for four target enzymes such as COX-2, mPGES-2, tyrosinase and HNE. Interestingly, we found that 4-hydroxyisoleucine has the potential to dock and bind with all of the eleven targeted enzymes. Conclusion: This present study has paved a new insight in understanding 4-hydroxyisoleucine as potential inhibitor against COX-2, mPGES-2, tyrosinase, HNE, MMP 2, MMP 9, XO, SQS, NOS, HAR and LOX.

AB - Background: The phytoconstituents phytic acid and 4-hydroxyisoleucine have been reported to posses various biological properties. Objective: This prompted us to carry out the docking study on these two ligands (phytic acid & 4-hydroxyisoleucine) against eleven targeted enzymes. Materials and Methods: Phytic acid & 4-hydroxyisoleucine were evaluated on the docking behaviour of cyclooxygenase-2 (COX-2), microsomal prostaglandin E synthase-2 (mPGES-2), tyrosinase, human neutrophil elastase (HNE), matrix metalloproteinase (MMP 2 and 9), xanthine oxidase (XO), squalene synthase (SQS), nitric oxide synthase (NOS), human aldose reductase (HAR) and lipoxygenase (LOX) using Discovery Studio Version 3.1 (except for LOX, where Autodock 4.2 tool was used). Results: Docking and binding free energy analysis revealed that phytic acid exhibited the maximum binding energy for four target enzymes such as COX-2, mPGES-2, tyrosinase and HNE. Interestingly, we found that 4-hydroxyisoleucine has the potential to dock and bind with all of the eleven targeted enzymes. Conclusion: This present study has paved a new insight in understanding 4-hydroxyisoleucine as potential inhibitor against COX-2, mPGES-2, tyrosinase, HNE, MMP 2, MMP 9, XO, SQS, NOS, HAR and LOX.

KW - 4-hydroxyisoleucine

KW - cyclooxygenase-2

KW - microsomal prostaglandin E synthase-2

KW - molecular docking

KW - phytic acid

KW - tyrosinase

UR - http://www.scopus.com/inward/record.url?scp=85032881678&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85032881678&partnerID=8YFLogxK

U2 - 10.4103/pm.pm_195_16

DO - 10.4103/pm.pm_195_16

M3 - Article

VL - 13

SP - S512-S518

JO - Pharmacognosy Magazine

JF - Pharmacognosy Magazine

SN - 0973-1296

IS - 51

ER -