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

dc.creatorArevalo, Fernando Javier
dc.creatorGonzález Techera, Andrés
dc.creatorZon, María Alicia
dc.creatorGonzález Sapienza, Gualberto
dc.creatorFernández, Héctor
dc.date2012-02
dc.date.accessioned2023-08-31T00:25:14Z
dc.date.available2023-08-31T00:25:14Z
dc.identifierhttp://hdl.handle.net/11336/199088
dc.identifierArevalo, 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
dc.identifier0956-5663
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8543409
dc.descriptionImmunosensors 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.
dc.descriptionFil: 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
dc.descriptionFil: González Techera, Andrés. Universidad de la República; Uruguay
dc.descriptionFil: 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
dc.descriptionFil: González Sapienza, Gualberto. Universidad de la República; Uruguay
dc.descriptionFil: Fernández, Héctor. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina
dc.formatapplication/pdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier Advanced Technology
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0956566311008141
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bios.2011.12.019
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subjectIMMUNOSENSOR
dc.subjectMOLINATE
dc.subjectPEPTIDE MIMICS
dc.subjectSQUARE WAVE VOLTAMMETRY
dc.subjecthttps://purl.org/becyt/ford/1.4
dc.subjecthttps://purl.org/becyt/ford/1
dc.titleUltra-sensitive electrochemical immunosensor using analyte peptidomimetics selected from phage display peptide libraries
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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