A critical review of advances in surface plasmon resonance imaging sensitivity

Liu, Chanjuan; Hu, Feichi; Yang, Wei; Xu, Jiying; Chen, Yi

doi:10.1016/j.trac.2017.10.001

Cited by 37 publications

(10 citation statements)

References 83 publications

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“…This may aid in the selection of appropriate binding pairs during immunoassay development. Careful observation of the binding curves in Figure 5 a and “difference” images seen in Figure 5 b–d indicate some ligands successfully bound to LF but not the complex formation of LTx [ 26 ], perhaps indicative that an epitope present on LF may be hidden upon the formation of the toxin.…”

Section: Resultsmentioning

confidence: 99%

Multiplexed, High-Sensitivity Measurements of Antibody Affinity Using Interferometric Reflectance Imaging Sensor

et al. 2021

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Anthrax lethal factor (LF) is one of the enzymatic components of the anthrax toxin responsible for the pathogenic responses of the anthrax disease. The ability to screen multiplexed ligands against LF and subsequently estimate the effective kinetic rates (kon and koff) and complementary binding behavior provides critical information useful in diagnostic and therapeutic development for anthrax. Tools such as biolayer interferometry (BLI) and surface plasmon resonance imaging (SPRi) have been developed for this purpose; however, these tools suffer from limitations such as signal jumps when the solution in the chamber is switched or low sensitivity. Here, we present multiplexed antibody affinity measurements obtained by the interferometric reflectance imaging sensor (IRIS), a highly sensitive, label-free optical biosensor, whose stability, simplicity, and imaging modality overcomes many of the limitations of other multiplexed methods. We compare the multiplexed binding results obtained with the IRIS system using two ligands targeting the anthrax lethal factor (LF) against previously published results obtained with more traditional surface plasmon resonance (SPR), which showed consistent results, as well as kinetic information previously unattainable with SPR. Additional exemplary data demonstrating multiplexed binding and the corresponding complementary binding to sequentially injected ligands provides an additional layer of information immediately useful to the researcher.

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Section: Resultsmentioning

confidence: 99%

Multiplexed, High-Sensitivity Measurements of Antibody Affinity Using Interferometric Reflectance Imaging Sensor

et al. 2021

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“…25 Despite these limitations, SPR is extremely popular due to being user-friendly and having broad applicability to various biomolecule classes. Given the large number of SPR publications, we refer here to reviews showcasing recent developments in SPR applications for protein-protein interaction quantification, [26][27][28] high-throughput with SPR imaging sensors (SPRi), 29 sensitivity and detection speed, 30,31 influence of capture surfaces, 32 and overcoming challenges with multi-valent binding. 33,34 Mamer et al, in their review, show SPR's convergence to cell-based protein-protein interaction measurements.…”

Section: Surface Plasmon Resonance (Spr)mentioning

confidence: 99%

Label-free methods for opticalin vitrocharacterization of protein–protein interactions

Soltermann

Struwe

Kukura

2021

Phys. Chem. Chem. Phys.

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“…So far, reflectivity-based SPRi has been widely used for high-throughput analysis in biosensing applications [27,28,29,30]. Nevertheless, reflectivity-based SPRi has become a high-throughput technique through compromising detection sensitivity due to the adoption of a less compact optical configuration, less sensitive mode of a single point intensity-based measurement, and commonly less-sensitive detectors [65]. Furthermore, for the detection of multiple interactions simultaneously, a homogeneous and optimal response for all sensing spots cannot be obtained with the choice of a unique operating point [31].…”

Section: Optical Configurations Of Sprimentioning

confidence: 99%

Recent Advances in Surface Plasmon Resonance Imaging Sensors

Wang

Loo

Chen

et al. 2019

Sensors

113

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The surface plasmon resonance (SPR) sensor is an important tool widely used for studying binding kinetics between biomolecular species. The SPR approach offers unique advantages in light of its real-time and label-free sensing capabilities. Until now, nearly all established SPR instrumentation schemes are based on single- or several-channel configurations. With the emergence of drug screening and investigation of biomolecular interactions on a massive scale these days for finding more effective treatments of diseases, there is a growing demand for the development of high-throughput 2-D SPR sensor arrays based on imaging. The so-called SPR imaging (SPRi) approach has been explored intensively in recent years. This review aims to provide an up-to-date and concise summary of recent advances in SPRi. The specific focuses are on practical instrumentation designs and their respective biosensing applications in relation to molecular sensing, healthcare testing, and environmental screening.

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A critical review of advances in surface plasmon resonance imaging sensitivity

Cited by 37 publications

References 83 publications

Multiplexed, High-Sensitivity Measurements of Antibody Affinity Using Interferometric Reflectance Imaging Sensor

Multiplexed, High-Sensitivity Measurements of Antibody Affinity Using Interferometric Reflectance Imaging Sensor

Label-free methods for opticalin vitrocharacterization of protein–protein interactions

Recent Advances in Surface Plasmon Resonance Imaging Sensors

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