Comparison of sensor structures for the signal amplification of surface plasmon resonance immunoassay using enzyme precipitation

Chih-Tsung Yang; Benjamin Thierry

doi:10.1117/12.2202554

22 December 2015 Comparison of sensor structures for the signal amplification of surface plasmon resonance immunoassay using enzyme precipitation

Chih-Tsung Yang, Benjamin Thierry

Author Affiliations +

Proceedings Volume 9668, Micro+Nano Materials, Devices, and Systems; 96682J (2015) https://doi.org/10.1117/12.2202554
Event: SPIE Micro+Nano Materials, Devices, and Applications, 2015, Sydney, New South Wales, Australia

Abstract

Surface plasmon resonance (SPR) biosensing has been successfully applied for the label-free detection of a broad range of bioanalytes ranging from bacteria, cell, exosome, protein and nucleic acids. When it comes to the detection of small molecules or analytes found at low concentration, amplification schemes are desirable to enhance binding signals and in turn increase sensitivity. A number of SPR signal amplification schemes have been developed and validated; however, little effort has been devoted to understanding the effect of the SPR sensor structures on the amplification of binding signals and therefore on the overall sensing performance. The physical phenomenon of long-range SPR (LRSPR) relies on the propagation of coupled surface plasmonic waves on the opposite sides of a nanoscale-thick noble metal film suspended between two dielectrics with similar refractive indices. Importantly, as compared with commonly used conventional SPR (cSPR), LRSPR is not only characterized by a longer penetration depth of the plasmonic waves in the analyzed medium but also by a greater sensitivity to bulk refractive index changes. In this work, an immunoassay signal amplification platform based on horseradish peroxidase (HRP) catalyzed precipitation was utilized to investigate the sensing performance with regards to cSPR and LRSPR. The enzymatic precipitation of 3, 3’-diaminobenzidine tetrahydrochloride (DAB)/H2O2 was used to amplify SPR signals. The structure-function relationship of cSPR and LRSPR sensors is presented for both standard refractometric measurements and the enzymatic precipitation scheme. Experimental data shows that despite its inherent higher sensitivity to bulk refractive index changes and higher figure of merit, LRSPR was characterized by a lower angular sensitivity in the model enzymatic amplification scheme used here.

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Chih-Tsung Yang and Benjamin Thierry "Comparison of sensor structures for the signal amplification of surface plasmon resonance immunoassay using enzyme precipitation", Proc. SPIE 9668, Micro+Nano Materials, Devices, and Systems, 96682J (22 December 2015); https://doi.org/10.1117/12.2202554

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