Toward sensitive immuno-based detection of tau protein by surface plasmon resonance coupled to carbon nanostructures as signal amplifiers

2017 ◽  
Vol 93 ◽  
pp. 289-292 ◽  
Author(s):  
S. Lisi ◽  
S. Scarano ◽  
S. Fedeli ◽  
E. Pascale ◽  
S. Cicchi ◽  
...  
2021 ◽  
pp. 115924
Author(s):  
Sepideh Najar-Ahmadi ◽  
Hossein Haghaei ◽  
Safar Farajnia ◽  
Reza Yekta ◽  
Jafar Ezzati Nazhad Dolatabadi ◽  
...  

Talanta ◽  
2008 ◽  
Vol 74 (4) ◽  
pp. 1038-1042 ◽  
Author(s):  
Mun’delanji Vestergaard ◽  
Kagan Kerman ◽  
Do-Kyun Kim ◽  
Ha Minh Hiep ◽  
Eiichi Tamiya

Bioimpacts ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 17-25
Author(s):  
Hossein Haghaei ◽  
Seyed Rafie Aref Hosseini ◽  
Somaieh Soltani ◽  
Farzaneh Fathi ◽  
Farzad Mokhtari ◽  
...  

<span style="color: #1f497d;">Introduction: Beta-Boswellic acid (BBA) is a pentacyclic terpene which has been obtained from frankincense and its beneficial effects on neurodegenerative disorders such as Alzheimer’s disease (AD) have been addressed.<br /> <span style="color: #1f497d;">Methods: In the present study, thermodynamic and kinetic aspects of BBA interaction with Tau protein as one of the important proteins involved in AD in the absence and presence of glucose has been investigated using surface plasmon resonance (SPR) method. Tau protein was immobilized onto the carboxy methyl dextran chip and its binding interactions with BBA were studied at physiological pH at various temperatures. Glucose interference with these interactions was also investigated.<br /> <span style="color: #1f497d;">Results: Results showed that BBA forms a stable complex with Tau (KD=8.45×10-7 M) at 298 K. Molecular modeling analysis showed a hydrophobic interaction between BBA and HVPGGG segment of R2 and R4 repeated domains of Tau.<br /> <span style="color: #1f497d;">Conclusion: The binding affinity increased by temperature enhancement, while it decreased significantly in the presence of glucose. Both association and dissociation of the BBA-Tau complex were accompanied with an entropic activation barrier; however, positive enthalpy and entropy changes revealed that hydrophobic bonding is the main force involved in the interaction.


2020 ◽  
pp. 44-49
Author(s):  
I. N. Pavlov

Two optical methods, namely surface plasmon resonance imaging and frustrated total internal reflection, are described in the paper in terms of comparing their sensitivity to change of refractive index of a thin boundary layer of an investigated medium. It is shown that, despite the fact that the theoretically calculated sensitivity is higher for the frustrated total internal reflection method, and the fact that usually in practice the surface plasmon resonance method, on the contrary, is considered more sensitive, under the same experimental conditions both methods show a similar result.


2010 ◽  
Vol 130 (7) ◽  
pp. 269-274 ◽  
Author(s):  
Takeshi Onodera ◽  
Takuzo Shimizu ◽  
Norio Miura ◽  
Kiyoshi Matsumoto ◽  
Kiyoshi Toko

PIERS Online ◽  
2008 ◽  
Vol 4 (7) ◽  
pp. 746-750 ◽  
Author(s):  
Bing-Hung Chen ◽  
Yih-Chau Wang ◽  
Jia-Hng Lin

2018 ◽  
Author(s):  
Yong Cao ◽  
Mark T. McDermott

<div> <div> <div> <p>Quantitative measurement of small-molecule metabolites is now emerging as an effective way to link the metabolite profile to disease state. Surface plasmon resonance (SPR) is a sensing platform that has demonstrated applicability for a large range of biomolecules. However, direct detection of small molecules with SPR challenges the refractive index based detection mechanism. Herein, we utilized an indirect detection format and developed an inhibition immunoassay for the quantitative measurement of 17β-estradiol (E2) using SPR. One competitor, BSA-E2 conjugate, was immobilized to the SPR chip via the reaction between the primary amino group of the conjugate and the succinimide group (NHS) introduced by the formation of a thiol-NHS monolayer on gold surface. Free E2 molecules compete with BSA-E2 on chip surface for binding sites provided by a monoclonal anti-E2 antibody. It was found the binding affinity of the antibody to BSA-E2 conjugate increases with decreasing surface coverage of BSA-E2 conjugate. Under optimal conditions, a sigmoidal calibration curve with a negative slope and a dynamic range from 10 pM to 2 nM was generated. The detection limit of the immunoassay is estimated to be 0.3 pM. Moreover, the immunoassay exhibits high specificity for E2 detection using estrone (E1) as a potential interference.</p></div></div></div>


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