SPR Biosensing MUA/Poly-L-lysine Platform for the Detection of 2,4-Dinitrophenol as Small Molecule Model System
| Autor: | David Emmanuel Romanin, Alejandro Fainstein, María L. Pedano, María Elena Vela, Cecilia Yamil Chain, Martín Rumbo, Guillermo Horacio Docena, Roberto Carlos Salvarezza, Andrea Crivaro, Eduardo Alejandro Ramirez, M. Antonieta Daza Millone, Jorgelina C. Montoya, Mauro D. Cocco |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Analyte
Identification Article Subject SPR Nanotechnology 02 engineering and technology Identificación 01 natural sciences purl.org/becyt/ford/1 [https] Non-competitive inhibition Biosensores Monolayer lcsh:Technology (General) Surface Plasmon Resonance assays purl.org/becyt/ford/1.4 [https] General Materials Science Surface plasmon resonance Molecular Biology Ciencias Exactas 2 4-dinitrofenol Poly-L-Lysine Chemistry Biosensing Otras Ciencias Químicas 010401 analytical chemistry Ciencias Químicas Surface-enhanced Raman spectroscopy 021001 nanoscience & nanotechnology Superficies Au-MUA-PLL Combinatorial chemistry Small molecule 0104 chemical sciences Biosensors Biología Molecular adsorption lcsh:T1-995 0210 nano-technology Biosensor CIENCIAS NATURALES Y EXACTAS Protein adsorption |
| Zdroj: | Journal of nanomaterials : Article ID 5432656. (2016) INTA Digital (INTA) Instituto Nacional de Tecnología Agropecuaria instacron:INTA CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET Journal of Nanomaterials, Vol 2016 (2016) SEDICI (UNLP) Universidad Nacional de La Plata instacron:UNLP |
| Popis: | 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. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas Instituto de Estudios Inmunológicos y Fisiopatológicos Facultad de Ciencias Exactas |
| Databáze: | OpenAIRE |
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