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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Series: | Journal of Nanomaterials |
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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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