Use of Surface Plasmon Resonance Coupled with Mass Spectrometry Reveals an Interaction between the Voltage-Gated Sodium Channel Type X α-Subunit and Caveolin-1

2008 ◽  
Vol 7 (12) ◽  
pp. 5333-5338 ◽  
Author(s):  
Elisabet Öhman ◽  
Anna Nilsson ◽  
Alexandra Madeira ◽  
Benita Sjögren ◽  
Per E. Andrén ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Surface Plasmon Resonance ◽  
Sodium Channel ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Voltage Gated Sodium Channel ◽  
Α Subunit ◽  
Caveolin 1 ◽  
Voltage Gated ◽  
Channel Type

scholarly journals A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif

2015 ◽  
Vol 145 (2) ◽  
pp. 155-162 ◽  
Author(s):  
Marie-France Martin-Eauclaire ◽  
Géraldine Ferracci ◽  
Frank Bosmans ◽  
Pierre E. Bougis
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Polarized Light ◽  
Voltage Sensor ◽  
Label Free ◽  
Fast Inactivation ◽  
Scorpion Toxins ◽  
Voltage Gated ◽  
Do So

Animal toxins that inhibit voltage-gated sodium (Nav) channel fast inactivation can do so through an interaction with the S3b–S4 helix-turn-helix region, or paddle motif, located in the domain IV voltage sensor. Here, we used surface plasmon resonance (SPR), an optical approach that uses polarized light to measure the refractive index near a sensor surface to which a molecule of interest is attached, to analyze interactions between the isolated domain IV paddle and Nav channel–selective α-scorpion toxins. Our SPR analyses showed that the domain IV paddle can be removed from the Nav channel and immobilized on sensor chips, and suggest that the isolated motif remains susceptible to animal toxins that target the domain IV voltage sensor. As such, our results uncover the inherent pharmacological sensitivities of the isolated domain IV paddle motif, which may be exploited to develop a label-free SPR approach for discovering ligands that target this region.

Optimizing the surface plasmon resonance/mass spectrometry interface for functional proteomics applications: How to avoid and utilize nonspecific adsorption

PROTEOMICS ◽  
2006 ◽  
Vol 6 (8) ◽  
pp. 2355-2364 ◽  
Author(s):  
Helén Larsericsdotter ◽  
Östen Jansson ◽  
Andrei Zhukov ◽  
Daphne Areskoug ◽  
Sven Oscarsson ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Functional Proteomics ◽  
Nonspecific Adsorption

Surface plasmon resonance-enabled mass spectrometry arrays

2006 ◽  
Vol 27 (18) ◽  
pp. 3671-3675 ◽  
Author(s):  
Dobrin Nedelkov ◽  
Kemmons A. Tubbs ◽  
Randall W. Nelson
Keyword(s):  
Mass Spectrometry ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance

scholarly journals Interactions of disulfide-deficient selenocysteine analogs of μ-conotoxin BuIIIB with the α-subunit of the voltage-gated sodium channel subtype 1.3

FEBS Journal ◽  
2014 ◽  
Vol 281 (13) ◽  
pp. 2885-2898 ◽  
Author(s):  
Brad R. Green ◽  
Min-Min Zhang ◽  
Sandeep Chhabra ◽  
Samuel D. Robinson ◽  
Michael J. Wilson ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Voltage Gated Sodium Channel ◽  
Α Subunit ◽  
Voltage Gated

scholarly journals The Interaction betweenEndopolygalacturonase fromFusarium moniliformeand PGIP fromPhaseolus vulgarisStudied by Surface Plasmon Resonance and Mass Spectrometry

2001 ◽  
Vol 2 (6) ◽  
pp. 359-364 ◽  
Author(s):  
Benedetta Mattei ◽  
Felice Cervone ◽  
Peter Roepstorff
Keyword(s):  
Mass Spectrometry ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Plant Cell Wall ◽  
Plant Defence ◽  
Limited Proteolysis ◽  
Specific Inhibitor ◽  
Phytopathogenic Fungi ◽  
Affinity Capture

A combination of surface plasmon resonance (SPR) and matrix-assisted laser-desorptionionization- time-of-flight mass spectrometry (MALDI-TOF-MS) was used to study the interaction betweenendopolygalacturonase (PG) fromFusarium moniliformeand a polygalacturonase-inhibiting protein (PGIP) fromPhaseolus vulgaris.PG hydrolyses the homogalacturonan of the plant cell wall and is considered an important pathogenicity factor of many fungi. PGIP is a specific inhibitor of fungal PGs and is thought to be involved in plant defence against phytopathogenic fungi. SPR was used either to study the effect of the PG glycosylation on the formation of the complex with PGIP, and as a sensitive affinity capture of an interacting peptide from a mixture of PG fragments obtained by limited proteolysis. Mass spectrometry allowed to characterise the interacting peptide eluted from the sensor surface.

Independent and synergistic interaction of retinal G-protein subunits with bovine rhodopsin measured by surface plasmon resonance

2001 ◽  
Vol 358 (2) ◽  
pp. 389-397 ◽  
Author(s):  
William A. CLARK ◽  
Xiaoying JIAN ◽  
Loren CHEN ◽  
John K. NORTHUP
Keyword(s):  
Surface Plasmon Resonance ◽  
G Protein ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Specific Activity ◽  
Receptor Interaction ◽  
Nucleotide Exchange ◽  
Α Subunit ◽  
Protein Subunits ◽  
Bovine Rhodopsin

We have used surface plasmon resonance (SPR) measurements for the kinetic analysis of G-protein-receptor interaction monitored in real time. Functionally active rhodopsin was immobilized on an SPR surface, with full retention of biochemical specific activity for catalysis of nucleotide exchange on the retinal G-protein α subunit, via binding to immobilized concanavalin A. The binding interactions of bovine retinal αt and β1γ1 subunits with rhodopsin measured by SPR were profoundly synergistic. Synergistic binding of the retinal G-protein subunits to rhodopsin was not observed for guanosine 5′-[γ-thio]triphosphate-bound Gαt, nor was binding observed with squid retinal Gαq, which is not activated by bovine rhodopsin. The binding affinity (336±171nM; mean value±S.D.) of retinal βγ for rhodopsin in the presence of retinal α subunit measured by SPR confirmed the apparent affinity of 254nM determined previously by nucleotide exchange assays. Binding of β1γ1, β1γ2, and β1γ8-olf dimers to rhodopsin, independently of the α subunit, was readily observable by SPR. Further, these dimers, differing only in their γ subunit compositions, displayed markedly distinct binding affinities and kinetics. The β1γ2 dimer bound with a kinetically determined Kd of 13±3nM, a value nearly identical with the biochemically determined K1/2 of 10nM. The physiologically appropriate β1γ1 displayed rapid association and dissociation kinetics, whereas the other β1γ dimers dissociated at a rate less than 1/100 as fast. Thus rhodopsin interaction with its native signalling partners is both rapid and transient, whereas the interaction of rhodopsin with heterologous Gβγ dimers is markedly prolonged. These results suggest that the duration of a G-protein-coupled receptor signalling event is an intrinsic property of the G-protein coupling partners; in particular, the βγ dimer.

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