surface plasmon resonance (SPR) Dotaz Zobrazit nápovědu
Surface plasmon resonance (SPR) biosensors are affinity sensing devices exploiting a special mode of electromagnetic field-surface plasmon-polariton-to detect the binding of analyte molecules from a liquid sample to biomolecular recognition elements immobilized on the surface of the sensor. In this paper, we review advances of SPR biosensor technology towards detection systems for the simultaneous detection of multiple analytes (multi-analyte detection). In addition, we report application of a recently developed multichannel SPR sensor based on spectroscopy of surface plasmons and wavelength division multiplexing of sensing channels to multi-analyte detection.
Lectin biochips and biosensors are used to detect and study the protein glycosylation. Glycosylation changes are accompanied by changes in physiological state, which may be associated with certain types of diseases such as cancer, rheumatoid arthritis, multiple sclerosis, etc. In recent years, this issue has been attracting more and more scientists and enormous advances have been achieved in this field. This work is focused on the use of surface plasmon resonance (SPR) in combination with lectin biosensors and biochips enabling tracking glycosylation and its changes. SPR is commonly used to detect proteins and to study the protein-protein and protein-drug interactions. Lectin SPR biochips additionally allow us to detect the glycan (glycoprotein)-lectin (protein) interactions. The great advantage of SPR, as compared to most other methods used for this purpose, is the possibility of real-time and label-free measurements. On the other hand, the measurement of large number of samples is time consuming. This is possible to overcome by using the SPR imaging (SPRi) techniques allowing simultaneous measurement of several samples. Practical applications of the lectin SPR biosensors and biochips are not only in biology and biomedicine research and diagnosis of diseases and detection of pathogenic microorganisms, but also in environmental monitoring, food control and even in the military for the detection of substances based on glycoprotein toxins.
We present a compact surface plasmon resonance (SPR) biosensor for the detection of bisphenol A (BpA), an endocrine-disrupting chemical. The biosensor is based on an SPR sensor platform (SPRCD) and the binding inhibition detection format. The detection of BpA in PBS and wastewater was performed at concentrations ranging from 0.05 to 1,000 ng/ml. The limit of detection for BpA in PBS and wastewater was estimated to be 0.08 and 0.14 ng/ml, respectively. It was also demonstrated that the biosensor can be regenerated for repeated use. Results achieved with the SPR biosensor are compared with those obtained using ELISA and HPLC methods.
To deal with the general problem of biomolecule specific binding analysis, we have applied the technique of difference spectra to the surface plasmon resonance (SPR)-enhanced total internal reflection ellipsometry measurement. We suggest a three-step treatment of the SPR background that can easily be integrated with the usual measurement routine. First, making use of the difference spectrum in ellipsometric angle Δ, single peak footprints of the topmost layer are obtained that facilitate its sensitive detection during film growth. Subsequently, circumventing the need for explicit knowledge of the substrate properties, the difference spectra peaks can be used for the end-point analysis of a binding. Finally, tracking the binding effectivity of the analyte we determine the injection speed and analyte concentration windows needed for successful monitoring of the film growth. We demonstrate our approach on a comprehensive two-stage binding experiment involving two biologically relevant molecules: the C-terminal domain (CTD) of RNA polymerase II and CTD-interacting domain of one of its transcription factors, the Rtt103 protein.
The process of DNA transposition involves the binding, cleavage, and recombination of specific DNA segments (transposable elements, TE) and is catalyzed by special enzymes encoded by the TE transposases. REP-associated tyrosine transposases (RAYTs) are a class of Y1 nucleases related to the IS200/IS605 transposases associated with a bacterial TE known as repetitive extragenic palindrome elements (REPs). Although RAYT has been subject of numerous studies, where DNA binding and cleavage by RAYT have been confirmed for Escherichia coli, the molecular mechanism of DNA insertion has not been fully understood. In this work, it is demonstrated that surface plasmon resonance (SPR) biosensor technology combined with a system of DNA hairpin probes (mimicking the natural REP sequence) and short oligonucleotides (ONs) can provide a rapid and real-time platform for monitoring and quantification of RAYT activity. We utilized RAYT from E. coli (strain MG1655) as a model system, where we evaluated its activity towards both a natural REP sequence as well as REP sequences having modifications targeting specific features of the DNA crucial for the DNA binding and cleavage. The characteristics of the RAYT-DNA interaction obtained by means of the SPR approach were compared with the results of SDS-PAGE analysis.
- MeSH
- biosenzitivní techniky přístrojové vybavení metody MeSH
- Escherichia coli enzymologie MeSH
- povrchová plasmonová rezonance přístrojové vybavení metody MeSH
- proteiny z Escherichia coli chemie genetika metabolismus MeSH
- regulace genové exprese enzymů fyziologie MeSH
- regulace genové exprese u bakterií fyziologie MeSH
- transposasy chemie genetika metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Bisphenol A (BpA) is a chemical that is extensively used in common plastic products, such as food and drink containers. It can leach from the plastics and penetrate into the human body, where it acts as an endocrine disruptor with significant risks to human health. In order to minimize the exposure of human populations to BpA, methods for the detection of BpA are needed. In this work, we present a novel surface plasmon resonance (SPR) biosensor for ultrasensitive detection of BpA. Our approach combines a binding inhibition assay with functionalized gold nanoparticles for the enhancement of sensor response. We demonstrate that the developed biosensor enables the detection of BpA in a wide range of concentrations (0.01 to 100,000 ng/mL) with an extremely low limit of detection-5.2 pg/mL.
Surface plasmon resonance (SPR) biosensors have become an important label-free optical biomolecular sensing technology and a "gold standard" for retrieving information on the kinetics of biomolecular interactions. Even though biomolecules typically contain an abundance of easily ionizable chemical groups, there is a gap in understanding of whether (and how) the electrostatic charge of a biomolecular system influences the SPR biosensor response. In this work we show that negative static charge present in a biomolecular layer on the surface of an SPR sensor results in significant SPR spectral shifts, and we identify two major mechanisms responsible for such shifts: 1) the formation of an electrical double layer (ionic mechanism), and 2) changes in the electron density at the surface of a metal (electronic mechanism). We show that under low ionic strength conditions, the electronic mechanism is dominant and the SPR wavelength shift is linearly proportional to the surface concentration of biomolecular charges. At high ionic strength conditions, both electric and ionic mechanisms contribute to the SPR wavelength shift. Using the electronic mechanism, we estimated the pKa of surface-bound carboxylic groups and the relative concentration of the carboxyl-terminated alkanethiols in a binary self-assembled monolayer of alkanethiols. The reported sensitivity of SPR to surface charge is especially important in the context of biomolecular sensing. Moreover, it provides an avenue for the application of SPR sensors for fast, label-free determination of the net charge of a biomolecular coating, which is of interest in material science, surface chemistry, electrochemistry, and other fields.
Surface plasmon resonance sensors have made vast advancements in the sensing technology and the number of applications achievable. New developments in surface plasmon resonance sensors have gained considerable momentum promoted by the urgent needs of fast, reliable and label-free methods for detection and quantification of analytes in molecular biology, medicine and other life sciences. However, even if enormous improvements in the limits of detections have been achieved, this technology still faces important challenges to be translated to clinical practice or in-field measurements. This paper reviews the important recent advances of this technology for the label-free detection in real biological samples and we discussed the key challenges to be overcome to transit from prototypes to commercial biosensors.
- MeSH
- biologie přístrojové vybavení metody MeSH
- diagnóza MeSH
- lidé MeSH
- povrchová plasmonová rezonance přístrojové vybavení metody MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
Surface plasmon resonance microscopy and imaging are optical methods that enable observation and quantification of interactions of nano- and microscale objects near a metal surface in a temporally and spatially resolved manner. This review describes the principles of surface plasmon resonance microscopy and imaging and discusses recent advances in these methods, in particular, in optical platforms and functional coatings. In addition, the biological applications of these methods are reviewed. These include the detection of a broad variety of analytes (nucleic acids, proteins, bacteria), the investigation of biological systems (bacteria and cells), and biomolecular interactions (drug-receptor, protein-protein, protein-DNA, protein-cell).
- MeSH
- Bacteria izolace a purifikace ultrastruktura MeSH
- design vybavení MeSH
- lidé MeSH
- mapování interakce mezi proteiny přístrojové vybavení metody MeSH
- mikroskopie přístrojové vybavení metody MeSH
- nukleové kyseliny analýza MeSH
- povrchová plasmonová rezonance přístrojové vybavení metody MeSH
- proteiny analýza MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH