Bioanalysis with surface plasmon resonance (original) (raw)
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Surface plasmon resonance as a bioanalytical tool
Journal of Molecular Structure, 1990
It is shown that Surface PLasmon Resonance is capable of detecting submonolayer quantities of proteins; information concerning the affinity of the surface can be obtained using this method. It is indicated how this method can be used to obtain more detailed information on the conformation of adsorbed macromolecules.
Surface Plasmon Resonance technology to assess biological interactions
Insights in Biology and Medicine, 2017
Molecular interactions between proteins or between proteins and small molecules are pivotal events for selective binding of biological structures and, consequentially, for their correct function. In this scenario, the evaluation of kinetic parameters, characterizing a molecular interactions, is considered a crucial event to reveal the nature of binding processes. The focus on peculiar forces involved in the molecular recognition represents an opportunity to explore biological interactions in real time, and to develop a number of innovative biotechnological methods for diagnosis and/or therapy. Currently, optical biosensors, offering an increasingly effective technology to detect in real time molecular binding, are usually composed by a detector, a sensor surface and a sample delivery system: only defi nite substances, which are able to interact specifi cally with the biological part, lead to an optical or electrical signal of the physical transducer. In this review we want to highlight the exponentially-growing interest of Surface Plasmon Resonance (SPR) based optical biosensors for molecular binding analysis in different research fi elds.
Surface Plasmon Resonance (SPR) Biosensors in Pharmaceutical Analysis
Critical Reviews in Analytical Chemistry, 2015
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On the Use of Surface Plasmon Resonance-Based Biosensors for Advanced Bioprocess Monitoring
Processes, 2021
Biomanufacturers are being incited by regulatory agencies to transition from a quality by testing framework, where they extensively test their product after their production, to more of a quality by design or even quality by control framework. This requires powerful analytical tools and sensors enabling measurements of key process variables and/or product quality attributes during production, preferably in an online manner. As such, the demand for monitoring technologies is rapidly growing. In this context, we believe surface plasmon resonance (SPR)-based biosensors can play a role in enabling the development of improved bioprocess monitoring and control strategies. The SPR technique has been profusely used to probe the binding behavior of a solution species with a sensor surface-immobilized partner in an investigative context, but its ability to detect binding in real-time and without a label has been exploited for monitoring purposes and is promising for the near future. In this r...
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.
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.
Reduction of nonspecific protein binding on surface plasmon resonance biosensors
Analytical and Bioanalytical Chemistry, 2006
Reduction of the nonspecific serum protein adsorption on a gold surface to levels low enough to allow the detection of biomarkers in complex media has been achieved using the N-hydroxysuccinimide (NHS) ester of 16-mercaptohexadecanoic acid. Carboxymethylated dextran (CM dextran), which is widely used, nonspecifically adsorbs enough proteins to mask the signal from target biomarkers in complex solutions such as serum or blood. The use of short-chain thiols greatly reduces the amount of nonspecific protein adsorption. Mixed layers of 11-mercaptoundecanoic acid or the NHS ester of 11-mercaptoundecanoic acid mixed layers with either 11-mercaptoundecanol or undecanethiol, and 16-mercaptohexadecanoic acid or the NHS ester of 16-mercaptohexadecanoic acid with hexadecanethiol, were also investigated for nonspecific protein binding properties as well as for biomarker signal response. The NHS ester of 16-mercaptohexadecanoic acid exhibits the largest signal for the biomarker myoglobin (including CM dextran) while offering a significantly diminished amount of nonspecific binding. The sensor has also been shown to detect interleukin-6 in cell culture media containing protein concentrations of at least 4 mg/mL.
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.