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

(2015) JOURNAL OF GENERAL PHYSIOLOGY. 145(2). p.155-162
Author
Organization
Abstract
Animal toxins that inhibit voltage-gated sodium (Na-v) 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 Na-v channel-selective. alpha-scorpion toxins. Our SPR analyses showed that the domain IV paddle can be removed from the Na-v 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.
Keywords
BETA-SCORPION TOXIN, DEPENDENT K+ CHANNEL, MOLECULAR DETERMINANTS, INTERACTION SITE, RECEPTOR-SITE, NA+ CHANNELS, DOMAIN-II, SENSOR, INACTIVATION, PHARMACOLOGY

Citation

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MLA
Martin-Eauclaire, Marie-France, Geraldine Ferracci, Frank Bosmans, et al. “A Surface Plasmon Resonance Approach to Monitor Toxin Interactions with an Isolated Voltage-gated Sodium Channel Paddle Motif.” JOURNAL OF GENERAL PHYSIOLOGY 145.2 (2015): 155–162. Print.
APA
Martin-Eauclaire, M.-F., Ferracci, G., Bosmans, F., & Bougis, P. E. (2015). A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif. JOURNAL OF GENERAL PHYSIOLOGY, 145(2), 155–162.
Chicago author-date
Martin-Eauclaire, Marie-France, Geraldine Ferracci, Frank Bosmans, and Pierre E Bougis. 2015. “A Surface Plasmon Resonance Approach to Monitor Toxin Interactions with an Isolated Voltage-gated Sodium Channel Paddle Motif.” Journal of General Physiology 145 (2): 155–162.
Chicago author-date (all authors)
Martin-Eauclaire, Marie-France, Geraldine Ferracci, Frank Bosmans, and Pierre E Bougis. 2015. “A Surface Plasmon Resonance Approach to Monitor Toxin Interactions with an Isolated Voltage-gated Sodium Channel Paddle Motif.” Journal of General Physiology 145 (2): 155–162.
Vancouver
1.
Martin-Eauclaire M-F, Ferracci G, Bosmans F, Bougis PE. A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif. JOURNAL OF GENERAL PHYSIOLOGY. 2015;145(2):155–62.
IEEE
[1]
M.-F. Martin-Eauclaire, G. Ferracci, F. Bosmans, and P. E. Bougis, “A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif,” JOURNAL OF GENERAL PHYSIOLOGY, vol. 145, no. 2, pp. 155–162, 2015.
@article{8584518,
  abstract     = {Animal toxins that inhibit voltage-gated sodium (Na-v) 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 Na-v channel-selective. alpha-scorpion toxins. Our SPR analyses showed that the domain IV paddle can be removed from the Na-v 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.},
  author       = {Martin-Eauclaire, Marie-France and Ferracci, Geraldine and Bosmans, Frank and Bougis, Pierre E},
  issn         = {0022-1295},
  journal      = {JOURNAL OF GENERAL PHYSIOLOGY},
  keywords     = {BETA-SCORPION TOXIN,DEPENDENT K+ CHANNEL,MOLECULAR DETERMINANTS,INTERACTION SITE,RECEPTOR-SITE,NA+ CHANNELS,DOMAIN-II,SENSOR,INACTIVATION,PHARMACOLOGY},
  language     = {eng},
  number       = {2},
  pages        = {155--162},
  title        = {A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif},
  url          = {http://dx.doi.org/10.1085/jgp.201411268},
  volume       = {145},
  year         = {2015},
}

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