Evaluation of potential molecular interaction between quorum sensing receptor, LuxP and grouper fatty acids: in-silico screening and simulation

Pathologically relevant behaviors of , such as the expression of virulence factors, biofilm production, and swarming motility, have been shown to be controlled by quorum sensing. The autoinducer-2 quorum sensing receptor protein LuxP is one of the target proteins for drug development to suppress the...

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Bibliographic Details
Published in:PeerJ (San Francisco, CA) CA), 2019-04, Vol.7, p.e6568, Article e6568
Main Authors: Low, Chen-Fei, Shamsir, Mohd Shahir, Mohamed-Hussein, Zeti-Azura, Baharum, Syarul Nataqain
Format: Article
Language:English
Subjects:
AI-2 quorum sensing
Amino acids
Analysis
Aquaculture
Aquaculture, Fisheries and Fish Science
Bacterial infections
Biofilms
Bioinformatics
Biosynthesis
Biotechnology
Bonds (Securities)
Cell signaling
Computational chemistry
Drug development
Enzymes
Fatty acids
Fish
Fishes
Free energy
Gene expression
Grouper metabolites
Hydrogen
Infections
Ligands
Metabolism
Metabolites
Molecular biology
Molecular dynamic analysis
Molecular dynamics
Molecular interaction
Proteins
Quorum sensing
Simulation
Studies
Swarming
Vibrio
Vibrio infections
Vibriosis
Virulence factors
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Summary:Pathologically relevant behaviors of , such as the expression of virulence factors, biofilm production, and swarming motility, have been shown to be controlled by quorum sensing. The autoinducer-2 quorum sensing receptor protein LuxP is one of the target proteins for drug development to suppress the virulence of . Here, we reported the potential molecular interaction of fatty acids identified in vibriosis-resistant grouper with LuxP. Fatty acid, 4-oxodocosahexaenoic acid (4R8) showed significant binding affinity toward LuxP (-6.0 kcal/mol) based on molecular docking analysis. The dynamic behavior of the protein-ligand complex was illustrated by molecular dynamic simulations. The fluctuation of the protein backbone, the stability of ligand binding, and hydrogen bond interactions were assessed, suggesting 4R8 possesses potential interaction with LuxP, which was supported by the low binding free energy (-29.144 kJ/mol) calculated using the molecular mechanics Poisson-Boltzmann surface area.
ISSN:2167-8359
2167-8359
DOI:10.7717/peerj.6568