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Handbook of Surface Plasmon Resonance CHAPTER 1 Introduction to Surface Plasmon Resonance

Handbook of Surface Plasmon Resonance CHAPTER 1 Introduction to Surface Plasmon Resonance

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CHAPTER 1
Introduction to Surface PlasmonResonance
ANNA J. TUDOS
a
AND RICHARD B.M. SCHASFOORT
b
a
Shell Global Solutions International BV, P.O. Box 380001030 BN Amsterdam, The Netherlands;
b
Biochip Group, MESA+ Institutefor Nanotechnology, Biomedical Technology Institute (BMTI), Faculty of Science and Engineering, University of Twente, P.O. Box 217,7500 AE Enschede, The Netherlands
1.1 What is Surface Plasmon Resonance?
Since its first observation by Wood in 1902 [1,2], the physical phenomenon of surface plasmon resonance (SPR) has found its way into practical applications insensitive detectors, capable of detecting sub-monomolecular coverage. What issurface plasmon resonance? Wood observed a pattern of ‘‘anomalous’’ dark andlight bands in the reflected light, when he shone polarized light on a mirror with adiffraction grating on its surface. Physical interpretation of the phenomenon wasinitiated by Lord Rayleigh [3], and further refined by Fano [4], but a completeexplanation of the phenomenon was not possible until 1968, when Otto [5] and inthe same year Kretschmann and Raether [6] reported the excitation of surfaceplasmons. Application of SPR-based sensors to biomolecular interaction mon-itoring was first demonstrated in 1983 by Liedberg
et al.
[7]. A historical overviewof the use of the phenomenon for biosensor applications is given in Section 1.3 of this chapter. To understand the excitation of surface plasmons, let us start with asimple experiment.
1.1.1 A Simple Experiment
Consider the experimental set-up depicted in Figure 1.1. When polarized light isshone through a prism on a sensor chip with a thin metal film on top, the lightwill be reflected by the metal film acting as a mirror. On changing the angle of incidence, and monitoring the intensity of the reflected light, the intensity of the
1
 
reflected light passes through a minimum (Figure 1.1, line A). At this angle of incidence, the light will excite surface plasmons, inducing surface plasmonresonance, causing a dip in the intensity of the reflected light. Photons of p-polarized light can interact with the free electrons of the metal layer, inducinga wave-like oscillation of the free electrons and thereby reducing the reflectedlight intensity.The angle at which the maximum loss of the reflected light intensity occurs iscalled resonance angle or SPR angle. The SPR angle is dependent on the opticalcharacteristics of the system,
e.g.
on the refractive indices of the media at bothsides of the metal, usually gold. While the refractive index at the prism side isnot changing, the refractive index in the immediate vicinity of the metal surfacewill change when accumulated mass (
e.g.
proteins) adsorb on it. Hence thesurface plasmon resonance conditions are changing and the shift of the SPRangle is suited to provide information on the kinetics of 
e.g.
protein adsorptionon the surface.
1.1.2 From Dip to Real-time Measurement
Surface plasmon resonance is an excellent method to monitor changes of therefractive index in the near vicinity of the metal surface. When the refractiveindex changes, the angle at which the intensity minimum is observed will shiftas indicated in Figure 1.2, where (A) depicts the original plot of reflected lightintensity
vs.
incident angle and (B) indicates the plot after the change inrefractive index. Surface plasmon resonance is not only suited to measure thedifference between these two states, but can also monitor the change in time, if one follows in time the shift of the resonance angle at which the dip is observed.
A
 
Angle (
ϕ
)BIntensity ofreflected light(%)
ϕ
Figure 1.1
Schematic experimental set-up of surface plasmon resonance excitation. Asensor chip with a gold coating is placed on a hemisphere (or prism).Polarized light shines from the light source (star) on the sensor chip.Reflected light intensity is measured in the detector (disk). At a certainangle of incidence (
j
), excitation of surface plasmons occurs, resulting in adip in the intensity of the reflected light (A). A change in refractive index atthe surface of the gold film will cause an angle shift from A to B.2
Chapter 1
 
Figure 1.2 depicts the shift of the dip in time, a so-called sensorgram. If thischange is due to a biomolecular interaction, the kinetics of the interaction canbe studied in real time.SPR sensors investigate only a very limited vicinity or fixed volume at themetal surface. The penetration depth of the electromagnetic field (so-calledevanescent field) at which a signal is observed typically does not exceed a fewhundred nanometers, decaying exponentially with the distance from the metallayer at the sensor surface. The penetration depth of the evanescent field is afunction of the wavelength of the incident light, as explained in Chapter 2.SPR sensors lack intrinsic selectivity: all refractive index changes in the evanes-cent field will be reflected in a change of the signal. These changes can be due torefractive index difference of the medium,
e.g.
a change in the buffer compositionor concentration; also, adsorption of material on the sensor surface can causerefractive index changes. The amount of adsorbed species can be determined afterinjection of the original baseline buffer, as shown in Figure 1.2. To permit selectivedetection at an SPR sensor, its surface needs to be modified with ligands suited forselective capturing of the target compounds but which are not prone to adsorbingany other components present in the sample or buffer media.
1.2 How to Construct an SPR Assay?
Now we have a basic understanding of the surface plasmon resonance signal andhow to measure it in time. We know that the sensor surface needs to be modifiedto allow selective capturing and thus selective measurement of a target compound.
AngleABTime (s)
Figure 1.2
A sensorgram: the angle at which the dip is observed
vs.
time. First, nochange occurs at the sensor and a baseline is measured with the dip at SPRangle (A). After injection of the sample (arrow) biomolecules will adsorb onthe surface resulting in a change in refractive index and a shift of the SPRangle to position B. The adsorption–desorption process can be followed inreal time and the amount of adsorbed species can be determined.3
Introduction to Surface Plasmon Resonance

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