Measurement of the localised plasmon penetration depth for gold nanoparticles using a non-invasive bio-stacking method

Read, T. A.; Olkhov, Rouslan V.; Shaw, Andrew M.

doi:10.1039/c3cp50758k

Cited by 17 publications

(19 citation statements)

References 26 publications

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“…The seed-printed array is removed from the printer and placed in a development solution to allow surface synthesis of the sensor surface nanoparticles. The resulting particles are typically 90 nm in diameter and have a surface coverage within each array element of approximately 10 % [20,23]. The nanoparticles are then functionalised in solution with a self-assembled monolayer (SAM) containing thiol group on one end for thiol-coupling to the Au surface and another end has either a linker (carboxyl group) for protein coupling or a spacer (alcohol group) in the ratio 1:10.…”

Section: Methodsmentioning

confidence: 99%

Label-free Fab and Fc affinity/avidity profiling of the antibody complex half-life for polyclonal and monoclonal efficacy screening

et al. 2015

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A unified approach to affinity screening for Fab and Fc interactions of an antibody for its antigen and FcγR receptor has been developed. An antigen array is used for the Fab affinity and cross-reactivity screening and protein A/G proxy is the FcγR receptor. The affinities are derived using a simple 1:1 binding model with a consistent error analysis. The association and dissociation kinetics are measured over optimised times for accurate determination. The Fab/Fc affinities are derived for ten antibodies: mAb-actin (mouse), pAb-BSA (sheep), pAb-collagen V (rabbit), pAb-CRP (goat), mAb-F1 (mouse), mAbs (mouse) 7.3, 12.3, 29.3, 36.3 and 46.3 raised against LcrV in Yersinia pestis. The rate of the dissociation of antigen-antibody complexes relates directly to their immunological function as does the Fc-FcγR complex and a new half-life plot has been defined with a Fab/Fc half-life range of 17-470 min. The upper half-life value points to surface avidity. Two antibodies that are protective as an immunotherapy define a Fab half-life >250 min and an Fc half-life >50 min as characteristics of ideal interactions which can form the basis of an antibody screen for immunotherapy.

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Section: Methodsmentioning

confidence: 99%

Label-free Fab and Fc affinity/avidity profiling of the antibody complex half-life for polyclonal and monoclonal efficacy screening

et al. 2015

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“…Figure 4(b) shows the local temperature immediately adjacent to the nanoparticle for different trapping laser powers calculated using Eqn. 2, where It is important to note that the LSPR is sensitive to changes only within the plasmon penetration depth, estimated to be of the order of the particle diameter [21,22], and so the effect is sensitive only to local changes in temperature.…”

Section: ⠀ 戀 ⤀ ⠀ 愀 ⤀mentioning

confidence: 99%

Intrinsic heating in optically trapped Au nanoparticles measured by dark-field spectroscopy

Andres-Arroyo¹,

Wang²,

Toe³

et al. 2015

Biomed. Opt. Express

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Assessing the degree of heating present when a metal nanoparticle is trapped in an optical tweezers is critical for its appropriate use in biological applications as a nanoscale force sensor. Heating is necessarily present for trapped plasmonic particles because of the non-negligible extinction which contributes to an enhanced polarisability. We present a robust method for characterising the degree of heating of trapped metallic nanoparticles, using the intrinsic temperature dependence of the localised surface plasmon resonance (LSPR) to infer the temperature of the surrounding fluid at different incident laser powers. These particle specific measurements can be used to infer the rate of heating and local temperature of trapped nanoparticles. Our measurements suggest a considerable amount of a variability in the degree of heating, on the range of 414-673 K/W, for different 100 nm diameter Au nanoparticles, and we associated this with variations in the axial trapping position.

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“…This value is consistent with the dissociation rate constant of goat IgG and protein G of k d ≈ 1 × 10 –4 s –1 , as has been measured by localized surface plasmon resonance (LSPR). 11 The association rate constants, on the other hand, show a significant variation for the different types of actuation. Compared to no actuation, a field gradient of ∼4 T/m (which corresponds to a single particle moving at a velocity of 12 μm/s) resulted in an increase in k a by a factor of 8 ± 4.…”

Section: Results and Discussionmentioning

confidence: 99%

How Actuated Particles Effectively Capture Biomolecular Targets

2017

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Because of their high surface-to-volume ratio and adaptable surface functionalization, particles are widely used in bioanalytical methods to capture molecular targets. In this article, a comprehensive study is reported of the effectiveness of protein capture by actuated magnetic particles. Association rate constants are quantified in experiments as well as in Brownian dynamics simulations for different particle actuation configurations. The data reveal how the association rate depends on the particle velocity, particle density, and particle assembly characteristics. Interestingly, single particles appear to exhibit target depletion zones near their surface, caused by the high density of capture molecules. The depletion effects are even more limiting in cases with high particle densities. The depletion effects are overcome and protein capture rates are enhanced by applying dynamic particle actuation, resulting in an increase in the association rate constants by up to 2 orders of magnitude.

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Measurement of the localised plasmon penetration depth for gold nanoparticles using a non-invasive bio-stacking method

Cited by 17 publications

References 26 publications

Label-free Fab and Fc affinity/avidity profiling of the antibody complex half-life for polyclonal and monoclonal efficacy screening

Label-free Fab and Fc affinity/avidity profiling of the antibody complex half-life for polyclonal and monoclonal efficacy screening

Intrinsic heating in optically trapped Au nanoparticles measured by dark-field spectroscopy

How Actuated Particles Effectively Capture Biomolecular Targets

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