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Interaction of POPC, DPPC, and POPE with the μ opioid receptor: A coarse-grained molecular dynamics study

Marie-Ange Angladon1, Mathieu Fossépré1, Laurence Leherte1

  • 1Laboratoire de Physico-Chimie Informatique, Unité de Chimie Physique Théorique et Structurale, Namur Medecine and Drug Innovation Center (NAMEDIC), Namur Research Institute for Life Sciences (NARILIS), University of Namur (UNamur), Namur, Belgium.

Plos One
|March 15, 2019
PubMed

Insights

The mu opioid receptor (μOR) structure is shaped by its surrounding lipids. Molecular dynamics simulations reveal distinct interactions between μOR and POPC, POPE, and DPPC lipids, influencing receptor conformation.

Area of Science:

  • Biophysics
  • Computational Chemistry
  • Pharmacology

Background:

  • The mu opioid receptor (μOR), a G protein-coupled receptor, is known to be modulated by its lipid environment.
  • Understanding these lipid-protein interactions is crucial for deciphering receptor function and drug development.

Purpose of the Study:

  • To investigate the lipid-induced modulation of the μOR.
  • To characterize the specific interactions between μOR and three distinct lipid types: POPC, POPE, and DPPC.

Main Methods:

  • Coarse-grained molecular dynamics (MD) simulations of μOR in three different membrane systems (POPC, POPE, DPPC) for a total of 45 μs.
  • Analysis of protein tilt, lipid-amino acid contacts, and the μOR-lipid interface network graph.

Main Results:

  • POPC lipids preferentially interact with μOR helices H1 and H5-H6.
  • POPE lipids show preferential interactions with helices H5-H6 and H6-H7.
  • DPPC lipids interact primarily with helices H4 and H6, demonstrating lipid-specific structural modulation of μOR.

Conclusions:

  • Different phospholipids distinctly modulate the structure and conformation of the μ opioid receptor.
  • The findings provide novel insights into the role of the lipid bilayer in regulating GPCR function.

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