scholarly journals Sensor Chip Using a Plasma-polymerized Film for Surface Plasmon Resonance Biosensors. Reliable Analysis of Binding Kinetics.

2000 ◽  
Vol 16 (4) ◽  
pp. 347-348 ◽  
Author(s):  
Hitoshi MUGURUMA ◽  
Ryohei NAGATA ◽  
Runa NAKAMURA ◽  
Kimiharu SATO ◽  
Shigeru UCHIYAMA ◽  
...  
2021 ◽  
Vol 1147 ◽  
pp. 23-29
Author(s):  
Chutiparn Lertvachirapaiboon ◽  
Akira Baba ◽  
Kazunari Shinbo ◽  
Keizo Kato

ACS Omega ◽  
2018 ◽  
Vol 3 (7) ◽  
pp. 7133-7140 ◽  
Author(s):  
Nur Selin Kaya ◽  
Anur Yadav ◽  
Michel Wehrhold ◽  
Laura Zuccaro ◽  
Kannan Balasubramanian

2021 ◽  
Author(s):  
◽  
Roshni Satheesh Babu

<p><b>Surface plasmon resonance (SPR) sensing is a label−free and rapid detection method and has extensive applications in the field of medical diagnostics, food control, and environmental monitoring. However, the lack of sensitivity to detect small molecules is a continuing concern in the application of this technique. Past research has explored different plasmonic structures such as metal nanoparticles, metallic nanoslits, nanoholes, colloidal Au nanoparticles, 2D nanomaterials, and multilayer structures as the sensing layer to improve the sensitivity of these sensors. However, the sensitivity improvement could be realised only with the cost of the increased complexity of optical configuration and sensor chip fabrication. Silver (Ag) is a very good candidate as the metallic layer for the sensor chip due to its higher electrical conductivity as compared to gold (Au). Besides cost−effectiveness, Ag thin film based sensors have better sensitivity with a sharp resonance dip and a high signal−to−noise ratio. However, the poor chemical stability of Ag thin films prevents their use in practical applications. Noble metals such as Au and platinum (Pt) offer greatly enhanced chemical stability. This work investigated the development of SPR sensors composed of a silver−noble metal bilayer structure to utilize both the sensitivity of silver and the chemical stability of the noble metal.</b></p> <p>To enable this research, an automated experimental SPR testbed for sensor characterisation was designed and constructed. This testbed is based on the Kretschmann configuration, using a He−Ne laser source at 632.8 nm. SPR sensor consisting of multilayer metal structures was fabricated using standard microelectronic fabrication techniques.</p> <p>The influence of the relative thickness of a noble metal capping layer on the SPR response and sensitivity from the Ag layer was systematically optimised, using both theoretical and experimental approaches. A theoretical analysis of the performance of the bimetallic SPR sensors was done using the transfer matrix method (TMM) by assuming a five−layer configuration. In the case of an Au capping layer, these simulations indicate an optimised thickness of 45 nm for Ag and 5 nm for Au. The observation from experimental analysis of different thickness combinations of Ag and Au matched the simulated results. However, the results of the stability studies exclude the practical use of 45 nm Ag/5 nm Au structures, as long−term degradation of the Ag layer occurs. A structure of 40 nm Ag/10nm Au was thus selected as the best composition for sensor applications. It is showed that sensors fabricated with this structure showed enhanced sensitivity compared to single−layer Au sensors, with a sensitivity 50% higher than that of the single−layer Au sensor. In the case of Ag/Pt structures, simulations indicated enhanced sensitivity from a 10 nm Ag/16 nm Pt structure. However, experimental measurements did not show any evidence for SPP excitation of Pt at the measured wavelength of 632.8 nm, making it unsuitable as a capping layer in our studies.</p> <p>The application of 40 nm Ag/10 nm Au bimetal layers as biosensors was done by the immobilization of thiol−terminated vitamin B12 aptamers on the Au sensor surface. However, the results were not reproducible, and more work on the binding kinetics of this aptamer will need to be performed to use this in a biosensor structure.</p>


2004 ◽  
Vol 186 (6) ◽  
pp. 1758-1768 ◽  
Author(s):  
Christoph Mader ◽  
Carina Huber ◽  
Dieter Moll ◽  
Uwe B. Sleytr ◽  
Margit Sára

ABSTRACT The interaction between S-layer protein SbsB and the secondary cell wall polymer (SCWP) of Geobacillus stearothermophilus PV72/p2 was investigated by real-time surface plasmon resonance biosensor technology. The SCWP is an acidic polysaccharide that contains N-acetylglucosamine, N-acetylmannosamine, and pyruvic acid. For interaction studies, recombinant SbsB (rSbsB) and two truncated forms consisting of either the S-layer-like homology (SLH) domain (3SLH) or the residual part of SbsB were used. Independent of the setup, the data showed that the SLH domain was exclusively responsible for SCWP binding. The interaction was found to be highly specific, since neither the peptidoglycan nor SCWPs from other organisms nor other polysaccharides were recognized. Data analysis from that setup in which 3SLH was immobilized on a sensor chip and SCWP represented the soluble analyte was done in accordance with a model that describes binding of a bivalent analyte to a fixed ligand in terms of an overall affinity for all binding sites. The measured data revealed the presence of at least two binding sites on a single SCWP molecule with a distance of about 14 nm and an overall K d of 7.7 × 10−7 M. Analysis of data from the inverted setup in which the SCWP was immobilized on a sensor chip was done in accordance with an extension of the heterogeneous-ligand model, which indicated the existence of three binding sites with low (K d = 2.6 × 10−5 M), medium (K d = 6.1 × 10−8 M), and high (K d = 6.7 × 10−11 M) affinities. Since in this setup 3SLH was the soluble analyte and the presence of small amounts of oligomers in even monomeric protein solutions cannot be excluded, the high-affinity binding site may result from avidity effects caused by binding of at least dimeric 3SLH. Solution competition assays performed with both setups confirmed the specificity of the protein-carbohydrate interaction investigated.


2000 ◽  
Vol 280 (1) ◽  
pp. 29-35 ◽  
Author(s):  
Eva-Maria Erb ◽  
Xinyong Chen ◽  
Stephanie Allen ◽  
Clive J. Roberts ◽  
Saul J.B. Tendler ◽  
...  

2017 ◽  
Vol 8 ◽  
pp. 03011
Author(s):  
Junpeng Tan ◽  
Bin Hao ◽  
Zhicheng Liu ◽  
Fengbo Bai ◽  
Ruiqin Yang ◽  
...  

2018 ◽  
Author(s):  
Federico Paoletti ◽  
Afaf El-Sagheer ◽  
Jun Allard ◽  
Tom Brown ◽  
Omer Dushek ◽  
...  

AbstractThe timely activation of homologous recombination is essential for the maintenance of genome stability, in which the RAD51 recombinase plays a central role. Biochemically, human RAD51 polymerises faster on single-stranded DNA (ssDNA) compared to double-stranded DNA (dsDNA), raising a key conceptual question: how does it discriminate between them? In this study, we tackled this problem by systematically assessing RAD51 binding kinetics on ssDNA and dsDNA differing in length and flexibility using surface plasmon resonance. By fitting detailed polymerisation models informed by our experimental datasets, we show that RAD51 is a mechano-sensor that exhibits a larger polymerisation rate constant on flexible ssDNA compared to rigid ssDNA or dsDNA. This model presents a new general framework suggesting that the flexibility of DNA, which may increase locally as a result of DNA damage, plays an important role in rapidly recruiting repair factors that multimerise at sites of DNA damage.


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