Plasmon resonance studies of agonist/antagonist binding to the human δ-opioid receptor

New structural insights into receptor-ligand interactions

Z. Salamon, S. Cowell, E. Varga, H. I. Yamamura, Victor J Hruby, G. Tollin

Research output: Contribution to journalArticle

85 Citations (Scopus)

Abstract

Structural changes accompanying the binding of ligands to the cloned human δ-opioid receptor immobilized in a solid-supported lipid bilayer have been investigated using coupled plasmon-waveguide resonance spectroscopy. This highly sensitive technique directly monitors mass density, conformation, and molecular orientation changes occurring in anisotropic thin films and allows direct determination of binding constants. Although both agonist binding and antagonist binding to the receptor cause increases in molecular ordering within the proteolipid membrane, only agonist binding induces an increase in thickness and molecular packing density of the membrane. This is a consequence of mass movements perpendicular to the plane of the bilayer occurring within the lipid and receptor components. These results are consistent with models of receptor function that involve changes in the orientation of transmembrane helices.

Original languageEnglish (US)
Pages (from-to)2463-2474
Number of pages12
JournalBiophysical Journal
Volume79
Issue number5
StatePublished - 2000

Fingerprint

Opioid Receptors
Ligands
Proteolipids
Molecular Conformation
Membranes
Lipid Bilayers
Spectrum Analysis
Lipids

ASJC Scopus subject areas

  • Biophysics

Cite this

Plasmon resonance studies of agonist/antagonist binding to the human δ-opioid receptor : New structural insights into receptor-ligand interactions. / Salamon, Z.; Cowell, S.; Varga, E.; Yamamura, H. I.; Hruby, Victor J; Tollin, G.

In: Biophysical Journal, Vol. 79, No. 5, 2000, p. 2463-2474.

Research output: Contribution to journalArticle

@article{ba1d5eb691f6480a998a257a4acea39b,
title = "Plasmon resonance studies of agonist/antagonist binding to the human δ-opioid receptor: New structural insights into receptor-ligand interactions",
abstract = "Structural changes accompanying the binding of ligands to the cloned human δ-opioid receptor immobilized in a solid-supported lipid bilayer have been investigated using coupled plasmon-waveguide resonance spectroscopy. This highly sensitive technique directly monitors mass density, conformation, and molecular orientation changes occurring in anisotropic thin films and allows direct determination of binding constants. Although both agonist binding and antagonist binding to the receptor cause increases in molecular ordering within the proteolipid membrane, only agonist binding induces an increase in thickness and molecular packing density of the membrane. This is a consequence of mass movements perpendicular to the plane of the bilayer occurring within the lipid and receptor components. These results are consistent with models of receptor function that involve changes in the orientation of transmembrane helices.",
author = "Z. Salamon and S. Cowell and E. Varga and Yamamura, {H. I.} and Hruby, {Victor J} and G. Tollin",
year = "2000",
language = "English (US)",
volume = "79",
pages = "2463--2474",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "5",

}

TY - JOUR

T1 - Plasmon resonance studies of agonist/antagonist binding to the human δ-opioid receptor

T2 - New structural insights into receptor-ligand interactions

AU - Salamon, Z.

AU - Cowell, S.

AU - Varga, E.

AU - Yamamura, H. I.

AU - Hruby, Victor J

AU - Tollin, G.

PY - 2000

Y1 - 2000

N2 - Structural changes accompanying the binding of ligands to the cloned human δ-opioid receptor immobilized in a solid-supported lipid bilayer have been investigated using coupled plasmon-waveguide resonance spectroscopy. This highly sensitive technique directly monitors mass density, conformation, and molecular orientation changes occurring in anisotropic thin films and allows direct determination of binding constants. Although both agonist binding and antagonist binding to the receptor cause increases in molecular ordering within the proteolipid membrane, only agonist binding induces an increase in thickness and molecular packing density of the membrane. This is a consequence of mass movements perpendicular to the plane of the bilayer occurring within the lipid and receptor components. These results are consistent with models of receptor function that involve changes in the orientation of transmembrane helices.

AB - Structural changes accompanying the binding of ligands to the cloned human δ-opioid receptor immobilized in a solid-supported lipid bilayer have been investigated using coupled plasmon-waveguide resonance spectroscopy. This highly sensitive technique directly monitors mass density, conformation, and molecular orientation changes occurring in anisotropic thin films and allows direct determination of binding constants. Although both agonist binding and antagonist binding to the receptor cause increases in molecular ordering within the proteolipid membrane, only agonist binding induces an increase in thickness and molecular packing density of the membrane. This is a consequence of mass movements perpendicular to the plane of the bilayer occurring within the lipid and receptor components. These results are consistent with models of receptor function that involve changes in the orientation of transmembrane helices.

UR - http://www.scopus.com/inward/record.url?scp=0033747206&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033747206&partnerID=8YFLogxK

M3 - Article

VL - 79

SP - 2463

EP - 2474

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 5

ER -