scholarly journals Site-Specific Immobilization of the Peptidoglycan Synthase PBP1B on a Surface Plasmon Resonance Chip Surface

ChemBioChem ◽  
2016 ◽  
Vol 17 (23) ◽  
pp. 2250-2256 ◽  
Author(s):  
Inge L. van't Veer ◽  
Nadia O. L. Leloup ◽  
Alexander J. F. Egan ◽  
Bert J. C. Janssen ◽  
Nathaniel I. Martin ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Chip Surface ◽  
Site Specific

scholarly journals Inside Cover: Site-Specific Immobilization of the Peptidoglycan Synthase PBP1B on a Surface Plasmon Resonance Chip Surface (ChemBioChem 23/2016)

ChemBioChem ◽  
2016 ◽  
Vol 17 (23) ◽  
pp. 2207-2207
Author(s):  
Inge L. van't Veer ◽  
Nadia O. L. Leloup ◽  
Alexander J. F. Egan ◽  
Bert J. C. Janssen ◽  
Nathaniel I. Martin ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Chip Surface ◽  
Site Specific

A Surface Plasmon Resonance Based Inhibition Immunoassay for Sensitive and Selective Detection of 17β-Estradiol

2018 ◽  
Author(s):  
Yong Cao ◽  
Mark T. McDermott
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Quantitative Measurement ◽  
Dynamic Range ◽  
Indirect Detection ◽  
Negative Slope ◽  
Chip Surface ◽  
Detection Mechanism ◽  
17Β Estradiol

<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>

scholarly journals Surface plasmon resonance biosensor for exosome detection based on reformative tyramine signal amplification activated by molecular aptamer beacon

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Wenqin Chen ◽  
Zhiyang Li ◽  
Wenqian Cheng ◽  
Tao Wu ◽  
Jia Li ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Signal Amplification ◽  
Lipid Membrane ◽  
Breast Cancer Patients ◽  
Her2 Positive ◽  
Chip Surface ◽  
Spr Biosensor ◽  
Aptamer Beacon

AbstractHuman epidermal growth factor receptor 2 (HER2)-positive exosomes play an extremely important role in the diagnosis and treatment options of breast cancers. Herein, based on the reformative tyramine signal amplification (TSA) enabled by molecular aptamer beacon (MAB) conversion, a label-free surface plasmon resonance (SPR) biosensor was proposed for highly sensitive and specific detection of HER2-positive exosomes. The exosomes were captured by the HER2 aptamer region of MAB immobilized on the chip surface, which enabled the exposure of the G-quadruplex DNA (G4 DNA) that could form peroxidase-like G4-hemin. In turn, the formed G4-hemin catalyzed the deposition of plentiful tyramine-coated gold nanoparticles (AuNPs-Ty) on the exosome membrane with the help of H2O2, generating a significantly enhanced SPR signal. In the reformative TSA system, the horseradish peroxidase (HRP) as a major component was replaced with nonenzymic G4-hemin, bypassing the defects of natural enzymes. Moreover, the dual-recognition of the surface proteins and lipid membrane of the desired exosomes endowed the sensing strategy with high specificity without the interruption of free proteins. As a result, this developed SPR biosensor exhibited a wide linear range from 1.0 × 104 to 1.0 × 107 particles/mL. Importantly, this strategy was able to accurately distinguish HER2-positive breast cancer patients from healthy individuals, exhibiting great potential clinical application. Graphical Abstract

Development of a Surface Plasmon Resonance–Based Immunoassay for Listeria monocytogenes

2005 ◽  
Vol 68 (4) ◽  
pp. 728-735 ◽  
Author(s):  
PAUL LEONARD ◽  
STEPHEN HEARTY ◽  
GARY WYATT ◽  
JOHN QUINN ◽  
RICHARD O'KENNEDY
Keyword(s):  
Surface Plasmon Resonance ◽  
Listeria Monocytogenes ◽  
Surface Plasmon ◽  
Polyclonal Antibody ◽  
Plasmon Resonance ◽  
Limit Of Detection ◽  
Chip Surface ◽  
Metal Affinity ◽  
Coefficients Of Variation ◽  
Internalin B

A polyclonal antibody was produced against Internalin B (InlB)–enriched extract and used to develop an inhibition assay to detect Listeria monocytogenes cells in solution using surface plasmon resonance. The gene sequence encoding for the InlB protein was cloned into a Qiagen pQE-60 vector, expressed in Escherichia coli, and purified by immobilized metal affinity chromatography. Protein G–purified anti-InlB–enriched extract polyclonal antibody was incubated with various concentrations of L. monocytogenes cells and subsequently injected over a purified-recombinant InlB (rInlB)–immobilized CM5 sensor chip surface. A decrease in antibody binding response was observed with increasing L. monocytogenes cell concentrations. Intraday and interday assay variability studies were carried out to evaluate precision and reproducibility. The assay had a limit of detection of less than 2 × 105 cells per ml and could be successfully reproduced with coefficients of variation of between 2.5 and 7.7%.

Screening the Biointeractions of Submicron Sized Particles Intended for Site-Specific Delivery Using Surface Plasmon Resonance

1999 ◽  
Vol 218 (2) ◽  
pp. 456-461 ◽  
Author(s):  
Simon L. McGurk ◽  
Martyn C. Davies ◽  
Clive J. Roberts ◽  
Saul J.B. Tendler ◽  
Philip M. Williams
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Site Specific

Highly Sensitive Surface Plasmon Resonance Sensor on Nanoscale Bioactive Surfaces for Specific Detection of Tri-Nitro Toluene

2006 ◽  
Vol 951 ◽  
Author(s):  
Praveen Singh ◽  
Takeshi Onodera ◽  
Kiyoshi Matsumoto ◽  
Norio Miura ◽  
Kiyoshi Toko
Keyword(s):  
Surface Plasmon Resonance ◽  
Detection Limit ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Self Assembly ◽  
Competitive Inhibition ◽  
Layer By Layer ◽  
Self Assembled Monolayer ◽  
Chip Surface ◽  
Resonance Sensor

ABSTRACTA nano-scale biosensor chip surface was fabricated using dinitro-phenylated key hole limpet (DNP-KLH) protein conjugate as ligand supported by underlying 11-amino 1-undecanethiol hydrochloride(AUT) self assembled monolayer (SAM) and bis sulfosuccinimidyl suberate(BS3) as crosslinker. Bioactive thin films were fabricated over gold chip via layer-by-layer self assembly methods. Biomolecular interaction between substrate specific anti-TNT antibody and DNP-KLH conjugate surface was monitored through surface plasmon resonance based optical sensor. The quantitation of tri-nitro toluene(TNT) on this bioactive surface was done using the solution based competitive inhibition assay. The DNP-KLH surface biosensor has shown a detection limit of 0.14 ng/ml(140 ppt) for TNT molecule. The detection limit of surface plasmon resonance(SPR) biosensor was further enhanced by using goat anti mouse antibody to the 0.002 ng/ml for TNT analyte. This TNT specific biosensor holds the promise to be one of most sensitive sensor surface under indirect competitive assay format. A short injection (12 sec) of 10 mM Glycine-HCl solution was found adequate for regeneration of DNP-KLH surface for repeated use.

Sign in / Sign up

Export Citation Format

Share Document