Surface Plasmon Resonance technology to assess biological interactions (original) (raw)
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Biomolecular interactions by Surface Plasmon Resonance technology
Annali dell'Istituto superiore di sanità, 2005
The Surface Plasmon Resonance (SPR) technique makes it possible to measure biomolecular interactions in real-time with a high degree of sensitivity and without the need of label. The information obtained is both qualitative and quantitative and it is possible to obtain the kinetic parameters of the interaction. This new technology has been used to study a diverse set of interaction partners of biological interest, such as protein-protein, protein-lipids, protein- nucleic acids or protein and low molecular weight molecules such as drugs, substrates and cofactors. In addition to basic biomedical research, the SPR biosensor has recently been used in food analysis, proteomics, immunogenicity and drug discovery.
The Biochemist, 2004
An understanding of the dynamics of biomolecular binding provides scientists with crucial information on the role of molecules in both health and disease. Whether it is antibodies recognizing antigens, cell-surface receptors binding to ligands, or if and how a potential drug candidate binds to its target, the ability to gather quality functional data on interactions is key. This is by no means a simple process. On top of the seemingly endless complexity of biomolecular interactions in the human body, many molecules need to be studied in a near-native environment. This places great demands on the technology used to study these systems. One technology that is capable of providing unique functional data on biomolecular interactions is surface plasmon resonance (SPR). SPR is currently being used for a wide variety of applications within drug development and life-science research, from proteomics to neurobiology and cancer, and even within the food industry. This article looks at the sci...
Analysis of Biomolecular Interactions Using a Miniaturized Surface Plasmon Resonance Sensor
Analytical Chemistry, 2002
A commercially available miniaturized surface plasmon resonance sensor has been investigated for its applicability to biological interaction analysis. The sensor was found to exhibit excellent repeatability and linearity for highrefractive index solutions and good reproducibility for the binding of proteins. Its detection limit for the monoclonal antibody M1 was found to be 2.1 fmol, which corresponds to a surface concentration of 21 pg/mm 2 . Simple surface immobilization procedures relying on biotin/avidin or glycoprotein/lectin chemistry have been explored. Equilibrium dissociation constants for the binding of the FLAG peptide to its monoclonal antibody (M1) and for the binding of concanavalin A to a glycoprotein have been determined. The close agreement of these measurements with values obtained by surface fluorescence microscopy and fluorescence correlation spectroscopy helps to validate the use of this device. Thus, this sensor shows promise as an inexpensive, portable, and accurate tool for bioanalytical applications in laboratory and clinical settings.
Surface Plasmon Resonance: Applications in Understanding Receptor–Ligand Interaction
Applied Biochemistry and Biotechnology, 2005
During last decade there has been significant progress in the development of analytical techniques for evaluation of receptor-ligand interaction. Surface plasmon resonance (SPR)-based optical biosensors are now being used extensively to define the kinetics of wide variety of macromolecular interactions and high-and low-affinity small molecule interactions. The experimental design data analysis methods are evolving along with widespread applications in ligand fishing, microbiology, virology, host-pathogen interaction, epitope mapping, and protein-, cell-, membrane-, nucleic acid-protein interactions. SPR-based biosensors have strong impact on basic and applied research significantly. This brief review describes the SPR technology and few of its applications in relation to receptor-ligand interaction that has brought significant change in the methodology, analysis, interpretation, and application of the SPR technology.
Determination of Affinity and Kinetic Rate Constants Using Surface Plasmon Resonance
Bacterial Toxins, 2000
Within the last three decades, surface plasmon resonance (SPR)-based optical biosensors have emerged as leading instruments for the study of biomolecular interactions. The rapid dissemination of the technology has provided researchers with versatile and sensitive instruments for the identification of kinetic and thermodynamic parameters related to macromolecular interactions. This review article presents the basic principles, as well as the classical experimental approaches and data treatment techniques related to the use of commercially available instruments for the characterization of protein-protein interactions. Emphasis will be put on new experimental trends aiming at improving two important aspects of any SPR kinetic studies, i.e., proteins tethering on biosensor surfaces as well as the optimization of data collection.
Analytical Biochemistry, 2000
were investigated with a view to providing a portable, inexpensive alternative to existing technologies for "real-time" biomolecular interaction analysis of whole cell-ligand interactions. A fiber optic SPR-based (FOSPR) biosensor, employing wavelength-dependent SPR, was constructed to enable continuous real-time data acquisition. In addition, a commercially available integrated angle-dependent SPR-based refractometer (ISPR) was modified to facilitate biosensing applications. Solid-phase detection of whole red blood cells (RBCs) using affinity-captured blood group specific antibodies was demonstrated using the BIACORE 1000, BIACORE Probe, FOSPR, and ISPR sensors. Nonspecific binding of RBCs to the hydrogel-based biointerface was negligible. However, the background noise level of the FOSPR-based biosensor was ϳ25-fold higher than that of the widely used BIACORE 1000 system while that of the ISPR-based biosensor was over 100-fold higher. Nevertheless, the FOSPR biosensor was suitable for the analysis of macromolecular analytes contained in crude matrices.
Localized surface plasmon resonance biosensors for real-time biomolecular binding study
A sensitive and low-cost microfluidic integrated biosensor is developed based on the localized surface plasmon resonance (LSPR) properties of gold nanoparticles, which allows label-free monitoring of biomolecular interactions in real-time. A novel quadrant detection scheme is introduced which continuously measures the change of the light transmitted through the nanoparticlecoated sensor surface. Using a green light emitting diode (LED) as a light source in combination with the quadrant detection scheme, a resolution of 10 −4 in refractive index units (RIU) is determined. This performance is comparable to conventional LSPR-based biosensors. The biological sensing is demonstrated using an antigen/antibody (biotin/ anti-biotin) system with an optimized gold nanoparticle film. The immobilization of biotin on a thiol-based selfassembled monolayer (SAM) and the subsequent affinity binding of anti-biotin are quantitatively detected by the microfluidic integrated biosensor and a detection limit of 270 ng/mL of anti-biotin was achieved. The microfluidic chip is capable of transporting a precise amount of biological samples to the detection areas to achieve highly sensitive and specific biosensing with decreased reaction time and less reagent consumption. The obtained results are compared with those measured by a surface plasmon resonance (SPR)-based Biacore system for the same binding event. This study demonstrates the feasibility of the integration of LSPR-based biosensing with microfluidic technologies, resulting in a low-cost and portable biosensor candidate compared to the larger and more expensive commercial instruments.
The Clinical biochemist. Reviews / Australian Association of Clinical Biochemists, 2012
Radioactive, chromogenic, fluorescent and other labels have long provided the basis of detection systems for biomolecular interactions including immunoassays and receptor binding studies. However there has been unprecedented growth in a number of powerful label free biosensor technologies over the last decade. While largely at the proof-of-concept stage in terms of clinical applications, the development of more accessible platforms may see surface plasmon resonance (SPR) emerge as one of the most powerful optical detection platforms for the real-time monitoring of biomolecular interactions in a label-free environment.In this review, we provide an overview of SPR principles and current and future capabilities in a diagnostic context, including its application for monitoring a wide range of molecular markers of disease. The advantages and pitfalls of using SPR to study biomolecular interactions are discussed, with particular emphasis on its potential to differentiate subspecies of ana...
Surface Plasmon Resonance: A Versatile Technique for Biosensor Applications
Sensors, 2015
Surface plasmon resonance (SPR) is a label-free detection method which has emerged during the last two decades as a suitable and reliable platform in clinical analysis for biomolecular interactions. The technique makes it possible to measure interactions in real-time with high sensitivity and without the need of labels. This review article discusses a wide range of applications in optical-based sensors using either surface plasmon resonance (SPR) or surface plasmon resonance imaging (SPRI). Here we summarize the principles, provide examples, and illustrate the utility of SPR and SPRI through example applications from the biomedical, proteomics, genomics and bioengineering fields. In addition, SPR signal amplification strategies and surface functionalization are covered in the review.
Applied biochemistry and biotechnology, 2005
During last decade there has been significant progress in the development of analytical techniques for evaluation of receptor-ligand interaction. Surface plasmon resonance (SPR)-based optical biosensors are now being used extensively to define the kinetics of wide variety of macromolecular interactions and high-and low-affinity small molecule interactions. The experimental design data analysis methods are evolving along with widespread applications in ligand fishing, microbiology, virology, host-pathogen interaction, epitope mapping, and protein-, cell-, membrane-, nucleic acid-protein interactions. SPR-based biosensors have strong impact on basic and applied research significantly. This brief review describes the SPR technology and few of its applications in relation to receptor-ligand interaction that has brought significant change in the methodology, analysis, interpretation, and application of the SPR technology.