Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries

Autores
Arevalo, Fernando Javier; González Techera, Andrés; Zon, María Alicia; González Sapienza, Gualberto; Fernández, Héctor
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Immunosensors for small analytes have been a great addition to the analytical toolbox due to their high sensitivity and extended analytical range. In these systems the analyte is detected when it competes for binding to the detecting antibody with a tracer compound. In this work we introduce the use of phage particles bearing peptides that mimic the target analyte as surrogates for conventional tracers. As a proof of concept, we developed a magneto-electrochemical immunosensor (EI) for the herbicide molinate and compare its performance with conventional formats. Using the same anti-molinate antibody and phage particles bearing a molinate peptidomimetic, the EI performed with an IC 50 of 0.15ngmL -1 (linear range from 4.4×10 -3 to 10ngmL -1). Compared to the conventional ELISA, the EI was faster (minutes), performed with a much wider linear range, and the detection limit that was 2500-fold lower. The EI produced consistent measurements and could be successfully used to assay river water samples with excellent recoveries. By using the same EI with a conventional tracer, we found that an important contribution to the gain in sensitivity is due to the filamentous structure of the phage (9×1000nm) which works as a multienzymatic tracer, amplifying the competitive reaction. Since phage-borne peptidomimetics can be selected from phage display libraries in a straightforward systematic manner and their production is simple and inexpensive, they can contribute to facilitate the development of ultrasensitive biosensors.
Fil: Arevalo, Fernando Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina
Fil: González Techera, Andrés. Universidad de la República; Uruguay
Fil: Zon, María Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina
Fil: González Sapienza, Gualberto. Universidad de la República; Uruguay
Fil: Fernández, Héctor. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina
Materia
IMMUNOSENSOR
MOLINATE
PEPTIDE MIMICS
SQUARE WAVE VOLTAMMETRY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/199088
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/199088
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide librariesArevalo, Fernando JavierGonzález Techera, AndrésZon, María AliciaGonzález Sapienza, GualbertoFernández, HéctorIMMUNOSENSORMOLINATEPEPTIDE MIMICSSQUARE WAVE VOLTAMMETRYhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Immunosensors for small analytes have been a great addition to the analytical toolbox due to their high sensitivity and extended analytical range. In these systems the analyte is detected when it competes for binding to the detecting antibody with a tracer compound. In this work we introduce the use of phage particles bearing peptides that mimic the target analyte as surrogates for conventional tracers. As a proof of concept, we developed a magneto-electrochemical immunosensor (EI) for the herbicide molinate and compare its performance with conventional formats. Using the same anti-molinate antibody and phage particles bearing a molinate peptidomimetic, the EI performed with an IC 50 of 0.15ngmL -1 (linear range from 4.4×10 -3 to 10ngmL -1). Compared to the conventional ELISA, the EI was faster (minutes), performed with a much wider linear range, and the detection limit that was 2500-fold lower. The EI produced consistent measurements and could be successfully used to assay river water samples with excellent recoveries. By using the same EI with a conventional tracer, we found that an important contribution to the gain in sensitivity is due to the filamentous structure of the phage (9×1000nm) which works as a multienzymatic tracer, amplifying the competitive reaction. Since phage-borne peptidomimetics can be selected from phage display libraries in a straightforward systematic manner and their production is simple and inexpensive, they can contribute to facilitate the development of ultrasensitive biosensors.Fil: Arevalo, Fernando Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; ArgentinaFil: González Techera, Andrés. Universidad de la República; UruguayFil: Zon, María Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; ArgentinaFil: González Sapienza, Gualberto. Universidad de la República; UruguayFil: Fernández, Héctor. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; ArgentinaElsevier Advanced Technology2012-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/199088Arevalo, Fernando Javier; González Techera, Andrés; Zon, María Alicia; González Sapienza, Gualberto; Fernández, Héctor; Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries; Elsevier Advanced Technology; Biosensors & Bioelectronics; 32; 1; 2-2012; 231-2370956-5663CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0956566311008141info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bios.2011.12.019info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:02:07Zoai:ri.conicet.gov.ar:11336/199088instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:02:07.696CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries
title Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries
spellingShingle Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries
Arevalo, Fernando Javier
IMMUNOSENSOR
MOLINATE
PEPTIDE MIMICS
SQUARE WAVE VOLTAMMETRY
title_short Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries
title_full Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries
title_fullStr Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries
title_full_unstemmed Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries
title_sort Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries
dc.creator.none.fl_str_mv Arevalo, Fernando Javier
González Techera, Andrés
Zon, María Alicia
González Sapienza, Gualberto
Fernández, Héctor
author Arevalo, Fernando Javier
author_facet Arevalo, Fernando Javier
González Techera, Andrés
Zon, María Alicia
González Sapienza, Gualberto
Fernández, Héctor
author_role author
author2 González Techera, Andrés
Zon, María Alicia
González Sapienza, Gualberto
Fernández, Héctor
author2_role author
author
author
author
dc.subject.none.fl_str_mv IMMUNOSENSOR
MOLINATE
PEPTIDE MIMICS
SQUARE WAVE VOLTAMMETRY
topic IMMUNOSENSOR
MOLINATE
PEPTIDE MIMICS
SQUARE WAVE VOLTAMMETRY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Immunosensors for small analytes have been a great addition to the analytical toolbox due to their high sensitivity and extended analytical range. In these systems the analyte is detected when it competes for binding to the detecting antibody with a tracer compound. In this work we introduce the use of phage particles bearing peptides that mimic the target analyte as surrogates for conventional tracers. As a proof of concept, we developed a magneto-electrochemical immunosensor (EI) for the herbicide molinate and compare its performance with conventional formats. Using the same anti-molinate antibody and phage particles bearing a molinate peptidomimetic, the EI performed with an IC 50 of 0.15ngmL -1 (linear range from 4.4×10 -3 to 10ngmL -1). Compared to the conventional ELISA, the EI was faster (minutes), performed with a much wider linear range, and the detection limit that was 2500-fold lower. The EI produced consistent measurements and could be successfully used to assay river water samples with excellent recoveries. By using the same EI with a conventional tracer, we found that an important contribution to the gain in sensitivity is due to the filamentous structure of the phage (9×1000nm) which works as a multienzymatic tracer, amplifying the competitive reaction. Since phage-borne peptidomimetics can be selected from phage display libraries in a straightforward systematic manner and their production is simple and inexpensive, they can contribute to facilitate the development of ultrasensitive biosensors.
Fil: Arevalo, Fernando Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina
Fil: González Techera, Andrés. Universidad de la República; Uruguay
Fil: Zon, María Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina
Fil: González Sapienza, Gualberto. Universidad de la República; Uruguay
Fil: Fernández, Héctor. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina
description Immunosensors for small analytes have been a great addition to the analytical toolbox due to their high sensitivity and extended analytical range. In these systems the analyte is detected when it competes for binding to the detecting antibody with a tracer compound. In this work we introduce the use of phage particles bearing peptides that mimic the target analyte as surrogates for conventional tracers. As a proof of concept, we developed a magneto-electrochemical immunosensor (EI) for the herbicide molinate and compare its performance with conventional formats. Using the same anti-molinate antibody and phage particles bearing a molinate peptidomimetic, the EI performed with an IC 50 of 0.15ngmL -1 (linear range from 4.4×10 -3 to 10ngmL -1). Compared to the conventional ELISA, the EI was faster (minutes), performed with a much wider linear range, and the detection limit that was 2500-fold lower. The EI produced consistent measurements and could be successfully used to assay river water samples with excellent recoveries. By using the same EI with a conventional tracer, we found that an important contribution to the gain in sensitivity is due to the filamentous structure of the phage (9×1000nm) which works as a multienzymatic tracer, amplifying the competitive reaction. Since phage-borne peptidomimetics can be selected from phage display libraries in a straightforward systematic manner and their production is simple and inexpensive, they can contribute to facilitate the development of ultrasensitive biosensors.
publishDate 2012
dc.date.none.fl_str_mv 2012-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/199088
Arevalo, Fernando Javier; González Techera, Andrés; Zon, María Alicia; González Sapienza, Gualberto; Fernández, Héctor; Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries; Elsevier Advanced Technology; Biosensors & Bioelectronics; 32; 1; 2-2012; 231-237
0956-5663
CONICET Digital
CONICET
url http://hdl.handle.net/11336/199088
identifier_str_mv Arevalo, Fernando Javier; González Techera, Andrés; Zon, María Alicia; González Sapienza, Gualberto; Fernández, Héctor; Ultra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries; Elsevier Advanced Technology; Biosensors & Bioelectronics; 32; 1; 2-2012; 231-237
0956-5663
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0956566311008141
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bios.2011.12.019
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Advanced Technology
publisher.none.fl_str_mv Elsevier Advanced Technology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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