Orientational binding modes of reporters in a viral-nanoparticle lateral flow assay

Kim, Jinsu; Poling-Skutvik, Ryan; Trabuco, João R. C.; Kourentzi, Katerina; Willson, Richard C.; Conrad, Jacinta C.

doi:10.1039/c6an00567e

Cited by 7 publications

(16 citation statements)

References 68 publications

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“…Biotinylated Fluor-phage were imaged in capillary-driven transport through the membrane using a sCMOS camera (pco.edge 4.2, 30 frame sec -1 , 30 ms exposure time, 208.3 μm × 213 μm image field of view). The position of the fluid interface scaled as the square root of time, 30 following Washburn's equation. 32 Recording began immediately after liquid breakthrough in the field of view ( t = 0 sec) and ceased when the phage particles exhibited only Brownian (rather than advective) motion, typically after six minutes.…”

Section: Methodsmentioning

confidence: 99%

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Increasing Binding Efficiency via Reporter Shape and Flux in a Viral Nanoparticle Lateral-Flow Assay

Kim

Kourentzi

et al. 2017

ACS Appl. Mater. Interfaces

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To identify factors controlling the performance of reporter particles in a sensitive lateral-flow assay (LFA), we investigated the effect of the flux and shape of filamentous bacteriophage (phage) on the performance of phage LFAs. Phage of three different lengths and diameters were modified with biotin and AlexaFluor 555 as binding and read-out elements, respectively. The binding efficiencies of the functionalized phage were tested in a fibrous glass LFA membrane modified with avidin. The total binding rate, quantified using real-time particle counting and particle image velocimetry, decreased monotonically with the average bulk flux of phage through the membrane. At the pore scale more phage bound in regions with faster local flow, confirming that both average and local flux increased binding. The number of bound phage increased with the aspect ratio of the phage and scaled with the phage surface area, consistent with a binding interaction controlled by the number of recognition elements on the surface. Together, these results indicate that increasing the likelihood that recognition elements on the surface of phage encounter the fibers enhances the assay binding efficiency and suggests one origin for the improved performance of nonspherical phage reporters.

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Section: Methodsmentioning

confidence: 99%

“…Recently, we showed that the flow field within an LFA membrane couples to the phage shape and promotes reorientation for binding, and hypothesized that binding efficiency can be increased by tuning the size and shape of reporters. 30 …”

Section: Introductionmentioning

confidence: 99%

Increasing Binding Efficiency via Reporter Shape and Flux in a Viral Nanoparticle Lateral-Flow Assay

Kim

Kourentzi

et al. 2017

ACS Appl. Mater. Interfaces

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“…As of March 2020 we did not find any scientific manuscript describing the development of a LFA using solely Fusion5, instead we found references using Fusion5 as part of LF strips or more complex structures. [172][173][174][175][176][177][178][179] Non-conventional materials. Other interesting low cost alternatives to the conventional LFAs membranes, such as cotton threads, cellulose and glass capillaries have been described in the last years.…”

Section: Assembly Of the Lfamentioning

confidence: 99%

Tutorial: design and fabrication of nanoparticle-based lateral-flow immunoassays

et al. 2020

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Lateral flow assays (LFA) are quick, simple and cheap assays to analyse a variety of samples at the point of care or in the field, making them one of the most widespread biosensors currently available. They have been successfully employed for the detection of a myriad of different targets (ranging from atoms up to whole cells) in all type of samples (including water, blood, foodstuff and environmental samples). Their operation relies on the capillary flow of the sample within a series of sequential pads with different functionalities aiming to generate a signal indicating the absence/presence (and, in some cases, the concentration) of the analyte of interest. In order to have a user-friendly operation, their development requires the optimization of multiple, interconnected parameters that may overwhelm new developers. In this Tutorial we provide the readers with: 1) the basic knowledge to understand the principles governing an LFA and to take informed decisions during lateral flow strip design and fabrication, 2) a roadmap for optimal LFA development independent of the specific application, 3) a step by step example protocol for the assembly and operation of an LF strip for the detection of Human Immunoglobulin G and 4) an extensive troubleshooting section addressing the most frequent issues in designing, assembling and using LFAs.

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“…The benefits of oriented binding of antibodies to magnetic nanoparticles through modification of antibodies' carbohydrate components were shown by Puertas et al using the example of LFIA for choriogonadotropin [46]. A comparison of methods of immobilization for receptors in bacteriophage-based LFIA is given in the works of Kim et al [47,48]. In particular, article [48] discussed the use of in vivo-biotinylated peptide for oriented immobilization of receptor molecules on a test strip.…”

Section: Proper Receptor For Lfiamentioning

confidence: 99%

“…A comparison of methods of immobilization for receptors in bacteriophage-based LFIA is given in the works of Kim et al [47,48]. In particular, article [48] discussed the use of in vivo-biotinylated peptide for oriented immobilization of receptor molecules on a test strip.…”

Section: Proper Receptor For Lfiamentioning

confidence: 99%

Ways to Reach Lower Detection Limits of Lateral Flow Immunoassays

Zherdev¹,

Dzantiev²

2018

Rapid Test - Advances in Design, Format and Diagnostic Applications

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This chapter considers factors influencing sensitivity of lateral flow immunoassay and modern developments that are focused on reaching lower detection limits. The existing variety of proposed approaches is classified in accordance with the "big five rules" for these assays, including proper sample, receptor, interaction, response, and output. The solutions for rapid extraction of target analytes and preventing negative influence of extractants are considered. Role to antibodies affinity and specificity is characterized. Potential of alternate bioreceptor molecules is discussed. Immunoreactants' compositions, concentrations, and locations on the test strip are characterized as factors determining assay parameters. The existing variety of labels is compared in terms of their optical and alternate registration. Tools to modulate a sequence of analytical reactions and to form aggregates of the detected labels are considered. The discussed approaches are illustrated through developments of test strips for detection of mycotoxins, veterinary drugs, and other analytes.The overall design of the immunochromatographic test strip is shown in Figure 1. It is a composite of several membranes of different structures and porosities, fixed on a support. The bundling of the test strip can vary, so it makes sense to consider its design based on what analytical tasks are being performed on its different sites.A. Typically, the lower portion of the test strip contains a sample pad. It ensures the absorption of sample components, in which the presence of the target analyte is checked.B. The following is a section with immunoreagents that are washed out during the analysis and move upward along with the components of the sample. As a rule, a conjugate pad forms this zone. It contains a conjugate of antibodies against the target analyte with a nanodispersed label-particles of colored latex, colloidal gold, and so on.The next two sections are located on the main working membrane of the test strip. C.First, there is a zone along which the movement of the absorbed components of the sample and the washed immunoreagents continues. During this movement, immune reactions occur, and specific intermolecular complexes are formed. D.Next, a mixture of reacted and unreacted molecules enters the binding area with immobilized immunoreagents. Depending on whether the target analyte was present in the sample and in what amount, binding of labeled immune complexes occurs in certain areas (in the traditional case, with the formation of narrow colored lines). Usually, additional reagents are located here to control the functionality of the test system. E. The upper part of the test strip with the final pad, usually structurally similar to the sample pad, ensures the further movement of the reaction mixture under the action of capillary forces and the washing of unreacted components from the underlying areas. These processes allow the label's binding to be evaluated correctly.Membrane components of the test strip are fixed on a plastic support and partia...

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Orientational binding modes of reporters in a viral-nanoparticle lateral flow assay

Cited by 7 publications

References 68 publications

Increasing Binding Efficiency via Reporter Shape and Flux in a Viral Nanoparticle Lateral-Flow Assay

Increasing Binding Efficiency via Reporter Shape and Flux in a Viral Nanoparticle Lateral-Flow Assay

Tutorial: design and fabrication of nanoparticle-based lateral-flow immunoassays

Ways to Reach Lower Detection Limits of Lateral Flow Immunoassays

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