Literature DB >> 17869585

Plasmon-waveguide resonance (PWR) spectroscopy for directly viewing rates of GPCR/G-protein interactions and quantifying affinities.

Victor J Hruby1, Gordon Tollin.   

Abstract

Plasmon-waveguide resonance (PWR) spectroscopy is an optical technique that has been developed in our laboratories and applied to the study of membrane-associated proteins, especially GPCRs. It has high sensitivity and requires no labeling of materials, and it can monitor changes in proteolipid mass density and conformation in real time using plasmon excitation by light polarized both perpendicular and parallel to the resonator surface. Direct measurements will be described of the association of ligands and G-proteins to GPCRs incorporated into a self-assembled lipid bilayer deposited on the silica surface of a PWR resonator. These studies have provided new insights into the functioning of this important class of signaling proteins.

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Year:  2007        PMID: 17869585      PMCID: PMC2151673          DOI: 10.1016/j.coph.2007.08.001

Source DB:  PubMed          Journal:  Curr Opin Pharmacol        ISSN: 1471-4892            Impact factor:   5.547


  17 in total

Review 1.  Plasmon resonance spectroscopy: probing molecular interactions within membranes.

Authors:  Z Salamon; M F Brown; G Tollin
Journal:  Trends Biochem Sci       Date:  1999-06       Impact factor: 13.807

2.  Binding of agonists, antagonists and inverse agonists to the human delta-opioid receptor produces distinctly different conformational states distinguishable by plasmon-waveguide resonance spectroscopy.

Authors:  Z Salamon; V J Hruby; G Tollin; S Cowell
Journal:  J Pept Res       Date:  2002-12

Review 3.  Plasmon-waveguide resonance spectroscopy: a new tool for investigating signal transduction by G-protein coupled receptors.

Authors:  Gordon Tollin; Zdzislaw Salamon; Scott Cowell; Victor J Hruby
Journal:  Life Sci       Date:  2003-11-14       Impact factor: 5.037

4.  Direct observation of G-protein binding to the human delta-opioid receptor using plasmon-waveguide resonance spectroscopy.

Authors:  Isabel D Alves; Zdzislaw Salamon; Eva Varga; Henry I Yamamura; Gordon Tollin; Victor J Hruby
Journal:  J Biol Chem       Date:  2003-09-30       Impact factor: 5.157

5.  Selectivity, cooperativity, and reciprocity in the interactions between the delta-opioid receptor, its ligands, and G-proteins.

Authors:  Isabel D Alves; Kathy A Ciano; Valentina Boguslavski; Eva Varga; Zdzislaw Salamon; Henry I Yamamura; Victor J Hruby; Gordon Tollin
Journal:  J Biol Chem       Date:  2004-08-17       Impact factor: 5.157

Review 6.  Functional selectivity and classical concepts of quantitative pharmacology.

Authors:  Jonathan D Urban; William P Clarke; Mark von Zastrow; David E Nichols; Brian Kobilka; Harel Weinstein; Jonathan A Javitch; Bryan L Roth; Arthur Christopoulos; Patrick M Sexton; Keith J Miller; Michael Spedding; Richard B Mailman
Journal:  J Pharmacol Exp Ther       Date:  2006-06-27       Impact factor: 4.030

Review 7.  Structural basis of function in heterotrimeric G proteins.

Authors:  William M Oldham; Heidi E Hamm
Journal:  Q Rev Biophys       Date:  2006-08-21       Impact factor: 5.318

8.  G-protein-coupled receptor screening technologies.

Authors:  Peter J Greasley; Frank P Jansen
Journal:  Drug Discov Today Technol       Date:  2005

9.  Plasmon-waveguide resonance studies of lateral segregation of lipids and proteins into microdomains (rafts) in solid-supported bilayers.

Authors:  Zdzislaw Salamon; Savitha Devanathan; Isabel D Alves; Gordon Tollin
Journal:  J Biol Chem       Date:  2005-01-24       Impact factor: 5.157

10.  Plasmon-waveguide resonance studies of ligand binding to the human beta 2-adrenergic receptor.

Authors:  Savitha Devanathan; Zhiping Yao; Zdzislaw Salamon; Brian Kobilka; Gordon Tollin
Journal:  Biochemistry       Date:  2004-03-23       Impact factor: 3.162

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  11 in total

Review 1.  The significance of G protein-coupled receptor crystallography for drug discovery.

Authors:  John A Salon; David T Lodowski; Krzysztof Palczewski
Journal:  Pharmacol Rev       Date:  2011-12       Impact factor: 25.468

Review 2.  Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery.

Authors:  Terry Kenakin; Laurence J Miller
Journal:  Pharmacol Rev       Date:  2010-04-14       Impact factor: 25.468

Review 3.  Cellular assays as portals to seven-transmembrane receptor-based drug discovery.

Authors:  Terry P Kenakin
Journal:  Nat Rev Drug Discov       Date:  2009-07-17       Impact factor: 84.694

Review 4.  New concepts in pharmacological efficacy at 7TM receptors: IUPHAR review 2.

Authors:  Terry Kenakin
Journal:  Br J Pharmacol       Date:  2013-02       Impact factor: 8.739

Review 5.  Signalling bias in new drug discovery: detection, quantification and therapeutic impact.

Authors:  Terry Kenakin; Arthur Christopoulos
Journal:  Nat Rev Drug Discov       Date:  2012-02-15       Impact factor: 84.694

6.  Origin and prediction of free-solution interaction studies performed label-free.

Authors:  Darryl J Bornhop; Michael N Kammer; Amanda Kussrow; Robert A Flowers; Jens Meiler
Journal:  Proc Natl Acad Sci U S A       Date:  2016-03-09       Impact factor: 11.205

7.  Sensitivity Comparison of Surface Plasmon Resonance and Plasmon-Waveguide Resonance Biosensors.

Authors:  Abdennour Abbas; Matthew J Linman; Quan Cheng
Journal:  Sens Actuators B Chem       Date:  2011-08-10       Impact factor: 7.460

Review 8.  Role of membrane integrity on G protein-coupled receptors: Rhodopsin stability and function.

Authors:  Beata Jastrzebska; Aleksander Debinski; Slawomir Filipek; Krzysztof Palczewski
Journal:  Prog Lipid Res       Date:  2011-03-22       Impact factor: 16.195

9.  Biased agonism.

Authors:  Terry Kenakin
Journal:  F1000 Biol Rep       Date:  2009-11-26

Review 10.  The potential for selective pharmacological therapies through biased receptor signaling.

Authors:  Terry Kenakin
Journal:  BMC Pharmacol Toxicol       Date:  2012-08-13       Impact factor: 2.483

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