A nanoscale optical biosensor: Sensitivity and selectivity of an approach based on the localized surface plasmon resonance spectroscopy of triangular silver nanoparticles

Amanda J. Haes, Richard P Van Duyne*

*Corresponding author for this work

Research output: Contribution to journalArticle

1789 Scopus citations

Abstract

Triangular silver nanoparticles (∼100 nm wide and 50 nm high) have remarkable optical properties. In particular, the peak extinction wavelength, λmax of their localized surface plasmon resonance (LSPR) spectrum is unexpectedly sensitive to nanoparticle size, shape, and local (∼10-30 nm) external dielectric environment. This sensitivity of the LSPR λmax to the nanoenvironment has allowed us to develop a new class of nanoscale affinity biosensors. The essential characteristics and operational principles of these LSPR nanobiosensors will be illustrated using the well-studied biotin-streptavidin system. Exposure of biotin-functionalized Ag nanotriangles to 100 nM streptavidin (SA) caused a 27.0 nm red-shift in the LSPR λmax. The LSPR λmax shift, ΔR/ΔRmax, versus [SA] response curve was measured over the concentration range 10-15 M < [SA] < 10-6 M. Comparison of the data with the theoretical normalized response expected for 1:1 binding of a ligand to a multivalent receptor with different sites but invariant affinities yielded approximate values for the saturation response, ΔRmax = 26.5 nm, and the surface-confined thermodynamic binding constant Ka,surf = 1011 M-1. At present, the limit of detection (LOD) for the LSPR nanobiosensor is found to be in the low-picomolar to high-femtomolar region. A strategy to amplify the response of the LSPR nanobiosensor using biotinylated Au colloids and thereby further improve the LOD is demonstrated. Several control experiments were performed to define the LSPR nanobiosensor's response to nonspecific binding as well as to demonstrate its response to the specific binding of another protein. These include the following: (1) electrostatic binding of SA to a nonbiotinylated surface, (2) nonspecific interactions of prebiotinylated SA to a biotinylated surface, (3) nonspecific interactions of bovine serum albumin to a biotinylated surface, and (4) specific binding of anti-biotin to a biotinylated surface. The LSPR nanobiosensor provides a pathway to ultrasensitive biodetection experiments with extremely simple, small, light, robust, low-cost instrumentation that will greatly facilitate field-portable environmental or point-of -service medical diagnostic applications.

Original languageEnglish (US)
Pages (from-to)10596-10604
Number of pages9
JournalJournal of the American Chemical Society
Volume124
Issue number35
DOIs
StatePublished - Sep 4 2002

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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