Cargando…
Surface Plasmon Resonance Biosensor Method for Palytoxin Detection Based on Na(+),K(+)-ATPase Affinity
Palytoxin (PLTX), produced by dinoflagellates from the genus Ostreopsis was first discovered, isolated, and purified from zoanthids belonging to the genus Palythoa. The detection of this toxin in contaminated shellfish is essential for human health preservation. A broad range of studies indicate tha...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3920252/ https://www.ncbi.nlm.nih.gov/pubmed/24379088 http://dx.doi.org/10.3390/toxins6010096 |
_version_ | 1782303142182912000 |
---|---|
author | Alfonso, Amparo Pazos, María-José Fernández-Araujo, Andrea Tobio, Araceli Alfonso, Carmen Vieytes, Mercedes R. Botana, Luis M. |
author_facet | Alfonso, Amparo Pazos, María-José Fernández-Araujo, Andrea Tobio, Araceli Alfonso, Carmen Vieytes, Mercedes R. Botana, Luis M. |
author_sort | Alfonso, Amparo |
collection | PubMed |
description | Palytoxin (PLTX), produced by dinoflagellates from the genus Ostreopsis was first discovered, isolated, and purified from zoanthids belonging to the genus Palythoa. The detection of this toxin in contaminated shellfish is essential for human health preservation. A broad range of studies indicate that mammalian Na(+),K(+)-ATPase is a high affinity cellular receptor for PLTX. The toxin converts the pump into an open channel that stimulates sodium influx and potassium efflux. In this work we develop a detection method for PLTX based on its binding to the Na(+),K(+)-ATPase. The method was developed by using the phenomenon of surface plasmon resonance (SPR) to monitor biomolecular reactions. This technique does not require any labeling of components. The interaction of PLTX over immobilized Na(+),K(+)-ATPase is quantified by injecting different concentrations of toxin in the biosensor and checking the binding rate constant (k(obs)). From the representation of k(obs) versus PLTX concentration, the kinetic equilibrium dissociation constant (K(D)) for the PLTX-Na(+),K(+)-ATPase association can be calculated. The value of this constant is K(D) = 6.38 × 10(−7) ± 6.67 × 10(−8) M PLTX. In this way the PLTX-Na(+),K(+)-ATPase association was used as a suitable method for determination of the toxin concentration in a sample. This method represents a new and useful approach to easily detect the presence of PLTX-like compounds in marine products using the mechanism of action of these toxins and in this way reduce the use of other more expensive and animal based methods. |
format | Online Article Text |
id | pubmed-3920252 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-39202522014-02-11 Surface Plasmon Resonance Biosensor Method for Palytoxin Detection Based on Na(+),K(+)-ATPase Affinity Alfonso, Amparo Pazos, María-José Fernández-Araujo, Andrea Tobio, Araceli Alfonso, Carmen Vieytes, Mercedes R. Botana, Luis M. Toxins (Basel) Article Palytoxin (PLTX), produced by dinoflagellates from the genus Ostreopsis was first discovered, isolated, and purified from zoanthids belonging to the genus Palythoa. The detection of this toxin in contaminated shellfish is essential for human health preservation. A broad range of studies indicate that mammalian Na(+),K(+)-ATPase is a high affinity cellular receptor for PLTX. The toxin converts the pump into an open channel that stimulates sodium influx and potassium efflux. In this work we develop a detection method for PLTX based on its binding to the Na(+),K(+)-ATPase. The method was developed by using the phenomenon of surface plasmon resonance (SPR) to monitor biomolecular reactions. This technique does not require any labeling of components. The interaction of PLTX over immobilized Na(+),K(+)-ATPase is quantified by injecting different concentrations of toxin in the biosensor and checking the binding rate constant (k(obs)). From the representation of k(obs) versus PLTX concentration, the kinetic equilibrium dissociation constant (K(D)) for the PLTX-Na(+),K(+)-ATPase association can be calculated. The value of this constant is K(D) = 6.38 × 10(−7) ± 6.67 × 10(−8) M PLTX. In this way the PLTX-Na(+),K(+)-ATPase association was used as a suitable method for determination of the toxin concentration in a sample. This method represents a new and useful approach to easily detect the presence of PLTX-like compounds in marine products using the mechanism of action of these toxins and in this way reduce the use of other more expensive and animal based methods. MDPI 2013-12-27 /pmc/articles/PMC3920252/ /pubmed/24379088 http://dx.doi.org/10.3390/toxins6010096 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Alfonso, Amparo Pazos, María-José Fernández-Araujo, Andrea Tobio, Araceli Alfonso, Carmen Vieytes, Mercedes R. Botana, Luis M. Surface Plasmon Resonance Biosensor Method for Palytoxin Detection Based on Na(+),K(+)-ATPase Affinity |
title | Surface Plasmon Resonance Biosensor Method for Palytoxin Detection Based on Na(+),K(+)-ATPase Affinity |
title_full | Surface Plasmon Resonance Biosensor Method for Palytoxin Detection Based on Na(+),K(+)-ATPase Affinity |
title_fullStr | Surface Plasmon Resonance Biosensor Method for Palytoxin Detection Based on Na(+),K(+)-ATPase Affinity |
title_full_unstemmed | Surface Plasmon Resonance Biosensor Method for Palytoxin Detection Based on Na(+),K(+)-ATPase Affinity |
title_short | Surface Plasmon Resonance Biosensor Method for Palytoxin Detection Based on Na(+),K(+)-ATPase Affinity |
title_sort | surface plasmon resonance biosensor method for palytoxin detection based on na(+),k(+)-atpase affinity |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3920252/ https://www.ncbi.nlm.nih.gov/pubmed/24379088 http://dx.doi.org/10.3390/toxins6010096 |
work_keys_str_mv | AT alfonsoamparo surfaceplasmonresonancebiosensormethodforpalytoxindetectionbasedonnakatpaseaffinity AT pazosmariajose surfaceplasmonresonancebiosensormethodforpalytoxindetectionbasedonnakatpaseaffinity AT fernandezaraujoandrea surfaceplasmonresonancebiosensormethodforpalytoxindetectionbasedonnakatpaseaffinity AT tobioaraceli surfaceplasmonresonancebiosensormethodforpalytoxindetectionbasedonnakatpaseaffinity AT alfonsocarmen surfaceplasmonresonancebiosensormethodforpalytoxindetectionbasedonnakatpaseaffinity AT vieytesmercedesr surfaceplasmonresonancebiosensormethodforpalytoxindetectionbasedonnakatpaseaffinity AT botanaluism surfaceplasmonresonancebiosensormethodforpalytoxindetectionbasedonnakatpaseaffinity |