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Surface Plasmon Resonance (SPR) Imaging Measurements

Surface plasmon resonance (SPR) reflectivity measurements are surface-sensitive, spectroscopic methods that can be used to characterize the thickness and/or index of refraction of ultrathin organic and biopolymer films at noble metal (Au, Ag, Cu) surfaces. Surface plasmon resonance spectroscopy has become widely used in the fields of chemistry and biochemistry to characterize biological surfaces and to monitor binding events. The success of these SPR measurements is primarily due to three factors: (i) with SPR spectroscopy the kinetics of biomolecular interactions can be measured in real time, (ii) the adsorption of unlabeled analyte molecules to the surface can be monitored, and (iii) SPR has a high degree of surface sensitivity that allows weakly bound interactions to be monitored in the presence of excess solution species. SPR spectroscopy has been used to monitor such events as antibody-antigen binding, DNA hybridization, and protein-DNA interactions.

While the vast majority of array-based studies of bioaffinity interactions employ fluorescently labeled biopolymers, there is a need for the continued development of sensitive analytical methods that can be used to detect bioaffinity interactions in biological samples without the need of molecular labels or tags. This is especially true for the case of protein-protein interactions, where labeling is difficult and can interfere with protein function. The surface-sensitive optical technique of surface plasmon resonance (SPR) imaging is emerging as a "label free" measurement that can be used in an array format for the detection of bioaffinity interactions. SPR imaging detects the presence of a biopolymer on a chemically modified gold surface by the change in the local index of refraction that occurs upon adsorption. In the past few years, we have developed the technique of near infrared SPR imaging for the detection of DNA and RNA by hybridization to DNA microarrays. We have also used SPR imaging of DNA microarrays to study protein-DNA interactions.


Some of our recent papers in this area:



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