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Title: SERS as a bioassay platform: fundamentals, design, and applications

Abstract

Bioanalytical science is experiencing a period of unprecedented growth. Drivers behind this growth include the need to detect markers central to human and veterinary diagnostics at ever-lower levels and greater speeds. A set of parallel arguments applies to pathogens with respect to bioterrorism prevention and food and water safety. This tutorial review outlines our recent explorations on the use of surface enhanced Raman scattering (SERS) for detection of proteins, viruses, and microorganisms in heterogeneous immunoassays. It will detail the design and fabrication of the assay platform, including the capture substrate and nanoparticle-based labels. The latter, which is the cornerstone of our strategy, relies on the construction of gold nanoparticles modified with both an intrinsically strong Raman scatterer and an antibody. This labelling motif, referred to as extrinsic Raman labels (ERLs), takes advantage of the well-established signal enhancement of scatterers when coated on nanometre-sized gold particles, whereas the antibody imparts antigenic specificity. We will also examine the role of plasmon coupling between the ERLs and capture substrate, and challenges related to particle stability, nonspecific adsorption, and assay speed.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Ames Laboratory (AMES), Ames, IA (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
974659
Report Number(s):
IS-J 7421
Journal ID: 1460-4744; TRN: US1002736
DOE Contract Number:  
DE-AC02-07CH11358
Resource Type:
Journal Article
Journal Name:
Chemical Society Reviews
Additional Journal Information:
Journal Volume: 37
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; ADSORPTION; BIOASSAY; CONSTRUCTION; DESIGN; DETECTION; FABRICATION; FOOD; GOLD; MICROORGANISMS; PATHOGENS; PLASMONS; PROTEINS; SAFETY; SCATTERING; SPECIFICITY; STABILITY; SUBSTRATES; VELOCITY; VIRUSES; WATER

Citation Formats

Porter, M, Lipert, R, Siperko, L, Wang, G, and Narayanan, R. SERS as a bioassay platform: fundamentals, design, and applications. United States: N. p., 2008. Web. doi:10.1039/b708461g.
Porter, M, Lipert, R, Siperko, L, Wang, G, & Narayanan, R. SERS as a bioassay platform: fundamentals, design, and applications. United States. doi:10.1039/b708461g.
Porter, M, Lipert, R, Siperko, L, Wang, G, and Narayanan, R. Tue . "SERS as a bioassay platform: fundamentals, design, and applications". United States. doi:10.1039/b708461g.
@article{osti_974659,
title = {SERS as a bioassay platform: fundamentals, design, and applications},
author = {Porter, M and Lipert, R and Siperko, L and Wang, G and Narayanan, R},
abstractNote = {Bioanalytical science is experiencing a period of unprecedented growth. Drivers behind this growth include the need to detect markers central to human and veterinary diagnostics at ever-lower levels and greater speeds. A set of parallel arguments applies to pathogens with respect to bioterrorism prevention and food and water safety. This tutorial review outlines our recent explorations on the use of surface enhanced Raman scattering (SERS) for detection of proteins, viruses, and microorganisms in heterogeneous immunoassays. It will detail the design and fabrication of the assay platform, including the capture substrate and nanoparticle-based labels. The latter, which is the cornerstone of our strategy, relies on the construction of gold nanoparticles modified with both an intrinsically strong Raman scatterer and an antibody. This labelling motif, referred to as extrinsic Raman labels (ERLs), takes advantage of the well-established signal enhancement of scatterers when coated on nanometre-sized gold particles, whereas the antibody imparts antigenic specificity. We will also examine the role of plasmon coupling between the ERLs and capture substrate, and challenges related to particle stability, nonspecific adsorption, and assay speed.},
doi = {10.1039/b708461g},
journal = {Chemical Society Reviews},
number = ,
volume = 37,
place = {United States},
year = {2008},
month = {3}
}