SPR Biosensing MUA/Poly-L-lysine Platform for the Detection of 2,4-Dinitrophenol as Small Molecule Model System

Surface Plasmon Resonance assays are being developed as alternative biodetection methods for a great number of pesticides and toxins. These substances typically have low molecular weight, making it necessary to perform competitive inhibition immunoassays. In most of the cases, the strategy is to imm...

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Main Authors: M. Antonieta Daza Millone, Eduardo A. Ramirez, Cecilia Y. Chain, Andrea Crivaro, David Romanin, Martín Rumbo, Guillermo Docena, Mauro D. Cocco, María L. Pedano, Alejandro Fainstein, Jorgelina Montoya, María E. Vela, R. C. Salvarezza
Format: Article
Language:English
Published: Hindawi Limited 2016-01-01
Series:Journal of Nanomaterials
Online Access:http://dx.doi.org/10.1155/2016/5432656
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spelling doaj-fe5bdbe386b2427e8669aeb6c6e760862020-11-24T20:56:17ZengHindawi LimitedJournal of Nanomaterials1687-41101687-41292016-01-01201610.1155/2016/54326565432656SPR Biosensing MUA/Poly-L-lysine Platform for the Detection of 2,4-Dinitrophenol as Small Molecule Model SystemM. Antonieta Daza Millone0Eduardo A. Ramirez1Cecilia Y. Chain2Andrea Crivaro3David Romanin4Martín Rumbo5Guillermo Docena6Mauro D. Cocco7María L. Pedano8Alejandro Fainstein9Jorgelina Montoya10María E. Vela11R. C. Salvarezza12Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas (CONICET-UNLP), CC16 Suc4, No. 1900, La Plata, Buenos Aires, ArgentinaInstituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas (CONICET-UNLP), CC16 Suc4, No. 1900, La Plata, Buenos Aires, ArgentinaInstituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas (CONICET-UNLP), CC16 Suc4, No. 1900, La Plata, Buenos Aires, ArgentinaInstituto de Estudios Inmunológicos y Fisiopatológicos (CONICET-UNLP), La Plata, ArgentinaInstituto de Estudios Inmunológicos y Fisiopatológicos (CONICET-UNLP), La Plata, ArgentinaInstituto de Estudios Inmunológicos y Fisiopatológicos (CONICET-UNLP), La Plata, ArgentinaInstituto de Estudios Inmunológicos y Fisiopatológicos (CONICET-UNLP), La Plata, ArgentinaCentro Atómico Bariloche, Instituto Balseiro, CNEA, 8400 S. C. de Bariloche, Rio Negro, ArgentinaCentro Atómico Bariloche, Instituto Balseiro, CNEA, 8400 S. C. de Bariloche, Rio Negro, ArgentinaCentro Atómico Bariloche, Instituto Balseiro, CNEA, 8400 S. C. de Bariloche, Rio Negro, ArgentinaEEA Anguil (INTA), Ruta Nac. No. 5 km 580, CC 11 (6326), Anguil, La Pampa, ArgentinaInstituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas (CONICET-UNLP), CC16 Suc4, No. 1900, La Plata, Buenos Aires, ArgentinaInstituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas (CONICET-UNLP), CC16 Suc4, No. 1900, La Plata, Buenos Aires, ArgentinaSurface Plasmon Resonance assays are being developed as alternative biodetection methods for a great number of pesticides and toxins. These substances typically have low molecular weight, making it necessary to perform competitive inhibition immunoassays. In most of the cases, the strategy is to immobilize a protein derivative of the analyte, which usually involves the appearance of nonspecific protein binding which limits the detection range of the assay. In this work we present results of a poly-L-lysine (Au-MUA-PLL) based sensor platform for quantitative determination of 2,4-dinitrophenol as model system for small molecular weight substances detection. The prepared sensor chip was characterized by means of Atomic Force Microscopy, Surface Plasmon Resonance, and Surface Enhanced Raman Spectroscopy. Experiments verified the absence of nonspecific protein adsorption to Au-MUA-PLL surfaces and the improvement of the competitive inhibition assays performance in comparison with single and mixed thiol self-assembled monolayers. The possibility of directly immobilizing 2,4-dinitrophenol to the poly-L-lysine containing platforms leads to an improvement in the detection of the soluble analyte by the competitive inhibition assay avoiding undesirable nonspecific protein adsorption. Therefore, Au-MUA-PLL surfaces constitute a suitable alternative for quantitative detection of small molecules when nonspecific adsorption cannot be avoided.http://dx.doi.org/10.1155/2016/5432656
collection DOAJ
language English
format Article
sources DOAJ
author M. Antonieta Daza Millone
Eduardo A. Ramirez
Cecilia Y. Chain
Andrea Crivaro
David Romanin
Martín Rumbo
Guillermo Docena
Mauro D. Cocco
María L. Pedano
Alejandro Fainstein
Jorgelina Montoya
María E. Vela
R. C. Salvarezza
spellingShingle M. Antonieta Daza Millone
Eduardo A. Ramirez
Cecilia Y. Chain
Andrea Crivaro
David Romanin
Martín Rumbo
Guillermo Docena
Mauro D. Cocco
María L. Pedano
Alejandro Fainstein
Jorgelina Montoya
María E. Vela
R. C. Salvarezza
SPR Biosensing MUA/Poly-L-lysine Platform for the Detection of 2,4-Dinitrophenol as Small Molecule Model System
Journal of Nanomaterials
author_facet M. Antonieta Daza Millone
Eduardo A. Ramirez
Cecilia Y. Chain
Andrea Crivaro
David Romanin
Martín Rumbo
Guillermo Docena
Mauro D. Cocco
María L. Pedano
Alejandro Fainstein
Jorgelina Montoya
María E. Vela
R. C. Salvarezza
author_sort M. Antonieta Daza Millone
title SPR Biosensing MUA/Poly-L-lysine Platform for the Detection of 2,4-Dinitrophenol as Small Molecule Model System
title_short SPR Biosensing MUA/Poly-L-lysine Platform for the Detection of 2,4-Dinitrophenol as Small Molecule Model System
title_full SPR Biosensing MUA/Poly-L-lysine Platform for the Detection of 2,4-Dinitrophenol as Small Molecule Model System
title_fullStr SPR Biosensing MUA/Poly-L-lysine Platform for the Detection of 2,4-Dinitrophenol as Small Molecule Model System
title_full_unstemmed SPR Biosensing MUA/Poly-L-lysine Platform for the Detection of 2,4-Dinitrophenol as Small Molecule Model System
title_sort spr biosensing mua/poly-l-lysine platform for the detection of 2,4-dinitrophenol as small molecule model system
publisher Hindawi Limited
series Journal of Nanomaterials
issn 1687-4110
1687-4129
publishDate 2016-01-01
description Surface Plasmon Resonance assays are being developed as alternative biodetection methods for a great number of pesticides and toxins. These substances typically have low molecular weight, making it necessary to perform competitive inhibition immunoassays. In most of the cases, the strategy is to immobilize a protein derivative of the analyte, which usually involves the appearance of nonspecific protein binding which limits the detection range of the assay. In this work we present results of a poly-L-lysine (Au-MUA-PLL) based sensor platform for quantitative determination of 2,4-dinitrophenol as model system for small molecular weight substances detection. The prepared sensor chip was characterized by means of Atomic Force Microscopy, Surface Plasmon Resonance, and Surface Enhanced Raman Spectroscopy. Experiments verified the absence of nonspecific protein adsorption to Au-MUA-PLL surfaces and the improvement of the competitive inhibition assays performance in comparison with single and mixed thiol self-assembled monolayers. The possibility of directly immobilizing 2,4-dinitrophenol to the poly-L-lysine containing platforms leads to an improvement in the detection of the soluble analyte by the competitive inhibition assay avoiding undesirable nonspecific protein adsorption. Therefore, Au-MUA-PLL surfaces constitute a suitable alternative for quantitative detection of small molecules when nonspecific adsorption cannot be avoided.
url http://dx.doi.org/10.1155/2016/5432656
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