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1.
Anal Chem ; 85(9): 4560-6, 2013 May 07.
Article in English | MEDLINE | ID: mdl-23560643

ABSTRACT

Localized surface plasmon resonance (LSPR) spectroscopy has been widely used for label-free, highly sensitive measurements of interactions at a surface. LSPR imaging (LSPRi) has the full advantages of LSPR but enables high-throughput, multiplexed measurements by simultaneously probing multiple individually addressable sensors on a single sample surface. Each spatially distinct sensor can be tailored to provide data regarding different surface functionalities or reaction environments. Previously, LSPRi has focused on single-particle sensing where the size scale is very small. Here, we create defined macroscale arrays of nanoparticles that are compatible with common patterning methods such as dip-pen nanolithography and multichannel microfluidic delivery devices. With this new LSPR sensing format, we report the first demonstration of multiplexed LSPR imaging and show that the increased throughput of our instrument enables the collection of a complete Langmuir binding curve on a single sensor surface. In addition, the multiplexed LSPR sensor is highly selective, as demonstrated by the hybridization of single-stranded DNA to complementary sequences immobilized on the sensor surface. The LSPR arrays described in this work exhibit uniform sensitivity and tailorable optical properties, making them an ideal platform for high-throughput, label-free analysis of a variety of molecular binding interactions.


Subject(s)
Biosensing Techniques , Biotin/chemistry , DNA/chemistry , Nanoparticles/chemistry , Surface Plasmon Resonance , Biosensing Techniques/instrumentation , Equipment Design , Molecular Structure , Surface Plasmon Resonance/instrumentation , Surface Properties
2.
J Opt Soc Am A Opt Image Sci Vis ; 29(6): 994-1002, 2012 Jun 01.
Article in English | MEDLINE | ID: mdl-22673431

ABSTRACT

In this paper, the theoretical sensitivity limit of the localized surface plasmon resonance (LSPR) to the surrounding dielectric environment is discussed. The presented theoretical analysis of the LSPR phenomenon is based on perturbation theory. Derived results can be further simplified assuming quasistatic limit. The developed theory shows that LSPR has a detection capability limit independent of the particle shape or arrangement. For a given structure, sensitivity is directly proportional to the resonance wavelength and depends on the fraction of the electromagnetic energy confined within the sensing volume. This fraction is always less than unity; therefore, one should not expect to find an optimized nanofeature geometry with a dramatic increase in sensitivity at a given wavelength. All theoretical results are supported by finite-difference time-domain calculations for gold nanoparticles of different geometries (rings, split rings, paired rings, and ring sandwiches). Numerical sensitivity calculations based on the shift of the extinction peak are in good agreement with values estimated by perturbation theory. Numerical analysis shows that, for thin (≤10 nm) analyte layers, sensitivity of the LSPR is comparable with a traditional surface plasmon resonance sensor and LSPR has the potential to be significantly less sensitive to temperature fluctuations.

3.
J Phys Chem C Nanomater Interfaces ; 115(5): 1410-1414, 2011 Feb 10.
Article in English | MEDLINE | ID: mdl-21660207

ABSTRACT

A method to amplify the wavelength shift observed from localized surface plasmon resonance (LSPR) bioassays is developed using gold nanoparticle-labeled antibodies. The technique, which involves detecting surface-bound analytes using gold nanoparticle conjugated antibodies, provides a way to enhance LSPR shifts for more sensitive detection of low-concentration analytes. Using the biotin and antibiotin binding pair as a model, we demonstrate up to a 400% amplification of the shift upon antibody binding to analyte. In addition, the antibody-nanoparticle conjugate improves the observed binding constant by 2 orders of magnitude, and the limit of detection by nearly 3 orders of magnitude. This amplification strategy provides a way to improve the sensitivity of plasmon-based bioassays, paving the way for single molecule-based detection and clinically relevant diagnostics.

4.
Nano Lett ; 11(3): 1098-105, 2011 Mar 09.
Article in English | MEDLINE | ID: mdl-21280643

ABSTRACT

The versatile optical and biological properties of a localized surface plasmon resonance (LSPR) sensor that responds to protein conformational changes are illustrated. The sensor detects conformational changes in a surface-bound construct of the calcium-sensitive protein calmodulin. Increases in calcium concentration induce a 0.96 nm red shift in the spectral position of the LSPR extinction maximum (λ(max)). Addition of a calcium chelating agent forces the protein to return to its original conformation and is detected as a reversal of the λ(max) shift. As opposed to previous work, this work demonstrates that these conformational changes produce a detectable shift in λ(max) even in the absence of a protein label, with a signal:noise ratio near 500. In addition, the protein conformational changes reversibly switch both the wavelength and intensity of the resonance peak, representing an example of a bimodal plasmonic component that simultaneously relays two distinct forms of optical information. This highly versatile plasmonic device acts as a biological sensor, enabling the detection of calcium ions with a biologically relevant limit of detection of 23 µM, as well as the detection of calmodulin-specific protein ligands.


Subject(s)
Biosensing Techniques , Surface Plasmon Resonance/instrumentation , Calmodulin/chemistry , Chelating Agents/chemistry , Ions , Molecular Conformation
5.
J Phys Chem C Nanomater Interfaces ; 113(15): 5891-5894, 2009 Mar 24.
Article in English | MEDLINE | ID: mdl-20161175

ABSTRACT

High resolution localized surface plasmon resonance (HR-LSPR) sensors were combined with matrix assisted laser desorption ionization mass spectrometry (MALDI-MS) for the first time. LSPR sensors provide real-time label-free detection of molecular adsorption. Subsequent MALDI-MS analysis enables identification of the adsorbed molecules. This synergistic LSPR-MS approach was applied to the detection and identification of amyloid beta oligomers which play an important role in the molecular pathogenesis of Alzheimer's Disease.

6.
Nat Mater ; 7(6): 442-53, 2008 Jun.
Article in English | MEDLINE | ID: mdl-18497851

ABSTRACT

Recent developments have greatly improved the sensitivity of optical sensors based on metal nanoparticle arrays and single nanoparticles. We introduce the localized surface plasmon resonance (LSPR) sensor and describe how its exquisite sensitivity to size, shape and environment can be harnessed to detect molecular binding events and changes in molecular conformation. We then describe recent progress in three areas representing the most significant challenges: pushing sensitivity towards the single-molecule detection limit, combining LSPR with complementary molecular identification techniques such as surface-enhanced Raman spectroscopy, and practical development of sensors and instrumentation for routine use and high-throughput detection. This review highlights several exceptionally promising research directions and discusses how diverse applications of plasmonic nanoparticles can be integrated in the near future.


Subject(s)
Biosensing Techniques , Metal Nanoparticles , Surface Plasmon Resonance/instrumentation , Sensitivity and Specificity
7.
J Am Chem Soc ; 130(18): 5836-7, 2008 May 07.
Article in English | MEDLINE | ID: mdl-18402443

ABSTRACT

A plasmonic switch based on the calcium-induced conformational changes of calmodulin is shown to exhibit reversible wavelength modulations in response to changing calcium concentration. The extinction maximum (lambdamax) of a localized surface plasmon resonance (LSPR) sensor functionalized with a novel calmodulin construct, cutinase-calmodulin-cutinase (CutCaMCut), reversibly shifts by 2-3 nm. A high-resolution (HR) LSPR spectrometer with a wavelength resolution (3sigma) of 1.5 x 10-2 nm was developed to detect these wavelength modulations in real-time, providing information about the dynamics and structure of the protein. The rate of conversion from open (Ca2+-bound) to closed (Ca2+-free) calmodulin is shown to be 4-fold faster than the reverse process, with a closing rate of 0.127 s-1 and opening rate of 0.034 s-1. As far as we are aware, this plasmonic switch marks the first use of LSPR spectroscopy to detect reversible conformational changes in an unlabeled protein.


Subject(s)
Calcium/chemistry , Calmodulin/chemistry , Calcium/metabolism , Calmodulin/metabolism , Carboxylic Ester Hydrolases/chemistry , Metal Nanoparticles/chemistry , Nanotechnology , Protein Conformation , Protein Structure, Tertiary , Silver/chemistry , Surface Plasmon Resonance/methods
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