Survey of the year 2001 commercial optical biosensor literature

Rich, Rebecca L.; Myszka, David G.

doi:10.1002/jmr.598

Cited by 101 publications

(40 citation statements)

References 693 publications

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“…After a period of silence, several SPR papers appeared on the topic of conformation-dependent sensing despite many considering the reports to be simply anomalous behavior (43)(44)(45)(46)(47), attributed to the following: (i) buffer mismatch, (ii) volume exclusion due to ligand density differences (43)(44)(45), (iii) nonspecific matrix interaction (46), and (iv) nonspecific reference interactions (47). Regardless, a recent paper reported that the RI sensing figures of merit were dependent on shape and the size of the Au nanoparticles (48) with sensitivities generally increasing as the nanoparticles became elongated and their apexes become sharper.…”

Section: Introductionmentioning

confidence: 99%

Origin and prediction of free-solution interaction studies performed label-free

Bornhop

Kammer

Kussrow

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Interaction/reaction assays have led to significant scientific discoveries in the biochemical, medical, and chemical disciplines. Several fundamental driving forces form the basis of intermolecular and intramolecular interactions in chemical and biochemical systems (London dispersion, hydrogen bonding, hydrophobic, and electrostatic), and in the past three decades the sophistication and power of techniques to interrogate these processes has developed at an unprecedented rate. In particular, label-free methods have flourished, such as NMR, mass spectrometry (MS), surface plasmon resonance (SPR), biolayer interferometry (BLI), and backscattering interferometry (BSI), which can facilitate assays without altering the participating components. The shortcoming of most refractive index (RI)-based label-free methods such as BLI and SPR is the requirement to tether one of the interaction entities to a sensor surface. This is not the case for BSI. Here, our hypothesis is that the signal origin for freesolution, label-free determinations can be attributed to conformation and hydration-induced changes in the solution RI. We propose a model for the free-solution response function (FreeSRF) and show that, when quality bound and unbound structural data are available, FreeSRF correlates well with the experiment (R 2 > 0.99, Spearman rank correlation coefficients >0.9) and the model is predictive within ∼15% of the experimental binding signal. It is also demonstrated that a simple mass-weighted dη/dC response function is the incorrect equation to determine that the change in RI is produced by binding or folding event in free solution.backscattering interferometry | assay methodology | molecular interactions | conformation change | hydration change C ontemporary assays enabling single-molecule detection (1,2) have accelerated the sequencing of the human genome (3) and facilitated imaging with extraordinary resolution without labels (4). To most closely approximate the natural state, an interaction assay methodology would interrogate the processes (reaction, molecular interaction, protein folding event, etc.) without perturbation. Label-free chemical and biochemical investigations (5, 6) transduce the desired signal without an exogenous label (fluorescent, radioactive, or otherwise) representing an essential step toward this goal. Many label-free methods require one of the interacting species to be either tethered or immobilized to the sensor surface, introducing a potential perturbation to the natural state of the species (7,8). However, back-scattering interferometry (BSI) is a free-solution label-free technique with the added benefit of sensitivity that rivals fluorescence (9). There are other techniques performed in free solution, such as MS (10, 11) and NMR (12,13) and the widely used isothermal titration calorimetry (ITC) (14, 15). As with NMR, ITC has many advantages, but exhibits modest sensitivity and often requires large sample quantities. Another increasingly popular free-solution approach is microscale thermophoresis (...

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Section: Introductionmentioning

confidence: 99%

Origin and prediction of free-solution interaction studies performed label-free

Bornhop

Kammer

Kussrow

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…[1,2] Major applications have been reported, not only for protein-protein interactions, including in conjunction with mass spectrometry, but also in SPR studies on nucleic acid-protein, carbohydrateprotein, and carbohydrate-carbohydrate interactions. [3][4][5][6] Qualitative SPR applications range from orphan-ligand and small-analyte screening to epitope mapping and complex assembly studies, whereas quantitative experiments include concentration measurements of active molecules in solution, evaluation of competition/inhibition events, and determination of rate and affinity constants. Nevertheless, since the SPR response is proportional to the accumulation of mass on the sensor surface, a serious constraint imposed by this technique concerns the dimensions of the molecules to be employed as analytes.…”

Section: Introductionmentioning

confidence: 99%

SPR Studies of Carbohydrate–Protein Interactions: Signal Enhancement of Low‐Molecular‐Mass Analytes by Organoplatinum(II)‐Labeling

et al. 2005

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The relatively insensitive surface plasmon resonance (SPR) signal detection of low‐molecular‐mass analytes that bind with weak affinity to a protein—for example, carbohydrate–lectin binding—is hampering the use of biosensors in interaction studies. In this investigation, low‐molecular‐mass carbohydrates have been labeled with an organoplatinum(II) complex of the type [PtCl(NCNR)]. The attachment of this complex increased the SPR response tremendously and allowed the detection of binding events between monosaccharides and lectins at very low analyte concentrations. The platinum atom inside the organoplatinum(II) complex was shown to be essential for the SPR‐signal enhancement. The organoplatinum(II) complex did not influence the specificity of the biological interaction, but both the signal enhancement and the different binding character of labeled compounds when compared with unlabeled ones makes the method unsuitable for the direct calculation of biologically relevant kinetic parameters. However, the labeling procedure is expected to be of high relevance for qualitative binding studies and relative affinity ranking of small molecules (not restricted only to carbohydrates) to receptors, a process of immense interest in pharmaceutical research.

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“…Comparing with the large variety of labeled methods, few label-free methods, such as optical [38,39] acoustic [40,41] and electrochemical analytical methods [42,43,44,45,46,47] could be applied to detect DNA hybridization. Label-free detection could remove experimental uncertainty induced by the effect of the label on molecular conformation, blocking of active binding epitopes, steric hindrance, inaccessibility of the labeling site, or the inability to find an appropriate label that functions equivalently for all molecules in an experiment, and greatly simplify the time and effort required for assay development, while removing experimental artifacts from quenching, shelf life and background fluorescence [48].…”

Section: Label-free Fiber-optic Dna Biosensorsmentioning

confidence: 99%

Recent advances in fiber-optic DNA biosensors

Wang¹,

Pang²,

Zhang³

2009

JBiSE

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Fiber-optic DNA biosensors are a kind of analytic setups, which convert the Waston-Crick base pairs matching duplex or Hoogsteen's triplex (T/A-T, C/G-C) formation into a readable analytical signals when functionalized singlestrands DNA (ssDNA) or double-strands DNA (dsDNA) of interest are immobilized on the surface of fiber-optic hybrids with target DNA or interacts with ligands. This review will provide the information about the fiber-optic DNA biosensors classified into two categories depending on the end fiber and side fiber with or without the labels-label-free fiber-optic DNA biosensors and labeled fiber-optic DNA biosensor in recent years. Both are dissertated, and emphasis is on the label-free fiber-optic DNA biosensors. Fiber-optic DNA biosensors had got great progresses because fiber-optic has more advantages over the other transducers and are easily processed by nanotechnology. So fiberoptic DNA biosensors have increasingly attracted more attention to research and develop the new fiber-optic DNA biosensors that integrated with the "nano-bio-info" technology for in vivo test, single molecular detection and on-line medical diagnosis. Finally, future prospects to the fiber-optic DNA biosensors are predicted.

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Survey of the year 2001 commercial optical biosensor literature

Cited by 101 publications

References 693 publications

Origin and prediction of free-solution interaction studies performed label-free

Origin and prediction of free-solution interaction studies performed label-free

SPR Studies of Carbohydrate–Protein Interactions: Signal Enhancement of Low‐Molecular‐Mass Analytes by Organoplatinum(II)‐Labeling

Recent advances in fiber-optic DNA biosensors

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