Surface Plasmon Resonance: A Versatile Technique for Biosensor Applications
<p>Concept of a surface plasmon resonance (SPR) biosensor: (<b>A</b>) Kretschmann geometry of the ATR method; (<b>B</b>) spectrum of reflected light before and after refractive index change; (<b>C</b>) analyte-biorecognition elements binding on SPR sensor surface and (<b>D</b>) refractive index changes caused by the molecular interactions in the reaction medium. Adapted from [<a href="#B30-sensors-15-10481" class="html-bibr">30</a>].</p> "> Figure 2
<p>General principle of surface plasmon resonance imaging (SPRI). (<b>Left</b>) The instrumentation of an SPR imaging system: The light source is a quartz tungsten-halogen lamp; the light is delivered through a liquid light guide to a goniometer arm, collimated by lenses, and passed through a narrow interference filter and a polarizer. A <span class="html-italic">p</span>-polarized and monochromatic light beam is then focused directly onto a prism coupler. The reflected light from the gold surface is captured by a monochromatic CCD camera. L2, L3 are lenses positioned in front of CCD for higher quality images. The images could be digitally stored using a B/W frame grabber and further analyzed using photography software; (<b>Right</b>) The analyte-ligand interaction shifts the SPR curve towards a higher angle (red to orange). Due to the measurement confinements (fixed wavelength and angle of incidence θ), changes in the reflectivity (Δ%R) at a single spot of the array can be simultaneously detected. Adapted from [<a href="#B32-sensors-15-10481" class="html-bibr">32</a>].</p> "> Figure 3
<p>High-throughput drug screening using an SPR imaging protein chip system. The bright image indicates protein-protein interaction on a gold surface. Upon the binding of an inhibitor to the target protein, protein-protein interactions are disrupted, resulting in changes in SPR imaging signal intensity and a darker image. Adapted from [<a href="#B62-sensors-15-10481" class="html-bibr">62</a>].</p> "> Figure 4
<p>Schematic representation of the PSA immunosensor based on PSA detection antibody-modified Au nanoparticles using surface plasmon resonance (SPR). For the PSA sandwich analysis, following PSA/tPSA bindingto the SPR sensor layer, 1.5 μg∙mL<sup>−1</sup> PSA detection antibody or Anti-PSA antibody conjugated AuNPs (20 nm, 5.1 × 1010 nanoparticles/mL or 40 nm, 5.1 × 1010 nanoparticles/mL) was injected on the surface. Adapted from [<a href="#B72-sensors-15-10481" class="html-bibr">72</a>].</p> "> Figure 5
<p>Schematic representation of DNA-directed immobilization. (<b>A</b>) Conjugation of four covalent conjugates (HA-HD) with the biotinylated antibodies anti-carcinoembryonic antigen (RAC), anti-ceruloplasmin (SAC), anti-complement-1-inactivator (SCI), and anti-lectin (GAL) to generate capture reagents A-RAC, B-SAC, C-SCI, and D-GAL. Adapted from [<a href="#B97-sensors-15-10481" class="html-bibr">97</a>]; (<b>B</b>) Conjugation of Streptavidin-Cy5 with biotinylated RAC, SAC, SCI and GAL for the use of a microscaled fluorescence immunoassay. Adapted from [<a href="#B97-sensors-15-10481" class="html-bibr">97</a>]; (<b>C</b>) DNA-directed immobilization of DNA-linked antibodies. c-A (Target sequence conjugated to anti-hCG): 5'-AGC GGA TAA CAA TTT CAC ACA GGA-3'; c-B (Target sequence conjugated to anti-hLH): 5'-AAC AGC TAT GAC CAT GAT TAC-3'; OEG, oligo (ethylene glycol). Adapted from [<a href="#B98-sensors-15-10481" class="html-bibr">98</a>].</p> "> Figure 6
<p>Schematic representation of direct immobilization of antibodies genetically modified with cysteines on a gold surface. A series of protein Gs containing two repeated IgG binding domains (B1 and B2) and a various numbers of cysteine amino acids, (Cys)<sub>1</sub>, (Cys)<sub>2</sub>, and (Cys)<sub>3</sub>, were genetically constructed, expressed/purified from <span class="html-italic">E. coli</span>, and subsequently analyzed using SPR biosensor. Adapted from [<a href="#B110-sensors-15-10481" class="html-bibr">110</a>].</p> "> Figure 7
<p>Schematic diagram of an immunochemical molecular recognition to illustrate the utility of Au colloid-enhanced biosensing. Two strategies for particle-enhanced SPR immunosensing are described: (<b>A</b>) Direct binding of the antigen-Au complex to an antibody-modified surface; (<b>B</b>) Antibody-modified surface followed by binding of a free antigen and then a secondary antibody-Au conjugate. Adapted from [<a href="#B112-sensors-15-10481" class="html-bibr">112</a>].</p> "> Figure 8
<p>Strategy for detecting SEB in buffer and stool using antibody-coated magnetic nanobeads. (<b>A</b>) Steps for processing samples with colloidal immunomagnetic beads (antibody-coated superparamagnetic nanobeads). Anti-SEB antibody-modified nanobeads were mixed with solutions containing the target antigen (SEB) prior to the SPR measurement; (<b>B</b>) SPR detection of staphylococcal enterotoxin B (SEB) in buffer (663 RIU), in stool (365 RIU), and unprocessed (7 RIU). Adapted from [<a href="#B115-sensors-15-10481" class="html-bibr">115</a>].</p> "> Figure 9
<p>The configuration of the proposed graphene-on-gold surface plasmon resonance biosensor based on generalized N-Layer model, where the gold film is deposited on top of a SF10 glass prism. A polychromatic light wave passes through the prism and is internally reflected on the prism-gold interface, creating an evanescent wave which penetrate the metal film (50 nm) and propagate along the x direction with propagation constant. The light propagation constant matches the surface plasmon polariton (SPP) propagation constant across the interface by controlling the incident angle θ. Plots of totally reflected intensity <span class="html-italic">versus</span> incident angle yield a peak, which is known as SPR angle. The graphene-on-gold surface plasmon resonance: prism | Au (50 nm) | graphene (L × 0.34 nm) | sensing medium, where L is the number of graphene layers, and Z<sub>0</sub> = 100 nm is the thickness of the biomolecule layer. Adapted from [<a href="#B116-sensors-15-10481" class="html-bibr">116</a>].</p> "> Figure 10
<p>SPR assay for ATP detection amplified by DNA-based hybridization chain reaction (HCR). (<b>A</b>) The S1-magnetic bead conjugates were prepared by direct immobilization of an amine-modified ATP aptamer linked to an activated carboxylate group on magnetic beads through the EDC/NHS chemistry, and then hybridized with its complementary oligonucleotide S2; (<b>B</b>) The strategy of continuous SPR monitoring of trigger DNA on a DNA chip array. Following a magnetic separation from the solution, the gold surface, on which the thiolated capture DNA was immobilized through S-Au bond, was treated with the sample containing S2. The released S2 functioned as trigger DNA to bind to the cohesive end of H1 in the presence of ATP. Adapted from [<a href="#B123-sensors-15-10481" class="html-bibr">123</a>].</p> "> Figure 11
<p>General principle of the objective-type SPRI setup. The optical configuration of the SPR microscope. Adapted from [<a href="#B133-sensors-15-10481" class="html-bibr">133</a>].</p> ">
Abstract
:1. Introduction
2. Operating Principle of SPR Biosensors
2.1. General Principle of SPR
2.2. SPR Imaging Principle
3. Applications of SPR-Based Biosensors
3.1. Biomedical Applications
3.1.1. Interaction Analyses
3.1.2. Conformational Change Studies
3.1.3. Mutation Detection
3.2. High-Throughput Screening (HTS)
3.3. Proteomics Researches
3.3.1. Tumor-Associated DNA Markers
3.3.2. Disease-Related Protein Biomarkers
3.4. Cellular Analysis and Cell-Based Detection
4. Immobilization of Biomolecules and Signal Amplification in SPR
4.1. Immobilization of Biomolecules
4.1.1. Covalent Coupling
4.1.2. Sequence-Specific DNA-Directed Immobilization of Proteins
4.1.3. Affinity Interactions
4.1.4. S-Au Bond in Cysteine-Gold Clusters
4.2. SPR Signal Amplification
4.2.1. Metal Nanoparticles
4.2.2. Magnetic Nanoparticles
4.2.3. Carbon-Based Nanomaterials
4.2.4. Other Approaches
5. Recent Advances of SPR Technology
6. Conclusions
Acknowledgments
Conflicts of Interest
References
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Nguyen, H.H.; Park, J.; Kang, S.; Kim, M. Surface Plasmon Resonance: A Versatile Technique for Biosensor Applications. Sensors 2015, 15, 10481-10510. https://doi.org/10.3390/s150510481
Nguyen HH, Park J, Kang S, Kim M. Surface Plasmon Resonance: A Versatile Technique for Biosensor Applications. Sensors. 2015; 15(5):10481-10510. https://doi.org/10.3390/s150510481
Chicago/Turabian StyleNguyen, Hoang Hiep, Jeho Park, Sebyung Kang, and Moonil Kim. 2015. "Surface Plasmon Resonance: A Versatile Technique for Biosensor Applications" Sensors 15, no. 5: 10481-10510. https://doi.org/10.3390/s150510481