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Plasmonic biosensors fabricated by galvanic displacement reactions for monitoring biomolecular interactions in real time
- Optical sensors are prepared by reduction of gold ions using freshly etched hydride-terminated porous silicon, and their ability to specifically detect binding between protein A/rabbit IgG and asialofetuin/Erythrina cristagalli lectin is studied. The fabrication process is simple, fast, and reproducible, and does not require complicated lab equipment. The resulting nanostructured gold layer on silicon shows an optical response in the visible range based on the excitation of localized surface plasmon resonance. Variations in the refractive index of the surrounding medium result in a color change of the sensor which can be observed by the naked eye. By monitoring the spectral position of the localized surface plasmon resonance using reflectance spectroscopy, a bulk sensitivity of 296 nm +/- 3 nm/RIU is determined. Furthermore, selectivity to target analytes is conferred to the sensor through functionalization of its surface with appropriate capture probes. For this purpose, biomolecules are deposited either by physical adsorption or byOptical sensors are prepared by reduction of gold ions using freshly etched hydride-terminated porous silicon, and their ability to specifically detect binding between protein A/rabbit IgG and asialofetuin/Erythrina cristagalli lectin is studied. The fabrication process is simple, fast, and reproducible, and does not require complicated lab equipment. The resulting nanostructured gold layer on silicon shows an optical response in the visible range based on the excitation of localized surface plasmon resonance. Variations in the refractive index of the surrounding medium result in a color change of the sensor which can be observed by the naked eye. By monitoring the spectral position of the localized surface plasmon resonance using reflectance spectroscopy, a bulk sensitivity of 296 nm +/- 3 nm/RIU is determined. Furthermore, selectivity to target analytes is conferred to the sensor through functionalization of its surface with appropriate capture probes. For this purpose, biomolecules are deposited either by physical adsorption or by covalent coupling. Both strategies are successfully tested, i.e., the optical response of the sensor is dependent on the concentration of respective target analyte in the solution facilitating the determination of equilibrium dissociation constants for protein A/rabbit IgG as well as asialofetuin/Erythrina cristagalli lectin which are in accordance with reported values in literature. These results demonstrate the potential of the developed optical sensor for cost-efficient biosensor applications.…
Author details: | Claudia PacholskiORCiDGND, Sophia RosencrantzGND, Ruben R. RosencrantzORCiDGND, Ruth Fabiola Balderas-ValadezGND |
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DOI: | https://doi.org/10.1007/s00216-020-02414-0 |
ISSN: | 1618-2642 |
ISSN: | 1618-2650 |
Pubmed ID: | https://pubmed.ncbi.nlm.nih.gov/32006063 |
Title of parent work (English): | Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica |
Publisher: | Springer |
Place of publishing: | Heidelberg |
Publication type: | Article |
Language: | English |
Date of first publication: | 2020/01/31 |
Publication year: | 2020 |
Release date: | 2023/04/17 |
Tag: | Biomolecular interactions; Gold nanostructure; Lectin; Localized surface plasmon resonance; Optical sensor; Surface functionalization |
Volume: | 412 |
Issue: | 14 |
Number of pages: | 13 |
First page: | 3433 |
Last Page: | 3445 |
Funding institution: | Heisenberg program from the German Research Foundation (DFG)German; Research Foundation (DFG) [426213922]; CONACyTConsejo Nacional de; Ciencia y Tecnologia (CONACyT) [CVU 264841, 291258]; Fraunhofer High; Performance Center for Functional lntegration in Materials |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie |
DDC classification: | 5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften |
Peer review: | Referiert |
Publishing method: | Open Access / Hybrid Open-Access |
License (German): | CC-BY - Namensnennung 4.0 International |