Plasmon-enhanced single-molecule enzymology

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Uittreksel

We present a numerical study on plasmon-enhanced single-molecule enzymology. We combine Brownian dynamics and electromagnetic simulations to calculate the enhancement of fluorescence signals of fluorogenic substrate converted by an enzyme conjugated to a plasmonic particle. We simulate the Brownian motion of a fluorescent product away from the active site of the enzyme, and calculate the photon detection rate taking into account modifications of the excitation and emission processes by coupling to the plasmon. We show that plasmon enhancement can boost the signal-to-noise ratio (SNR) of single turnovers by up to 100 fold compared to confocal microscopy. This enhancement factor is a trade-off between the reduced residence time in the near-field of the particle, and the enhanced emission intensity due to coupling to the plasmon. The enhancement depends on the size, shape and material of the particle and the photophysical properties of the fluorescent product. Our study provides guidelines on how to enhance the SNR of single-molecule enzyme studies and may aid in further understanding and quantifying static and dynamic heterogeneity.
TaalEngels
Pagina's3073–3081
TijdschriftACS Photonics
Volume5
Nummer van het tijdschrift8
DOI's
StatusGepubliceerd - 23 mei 2018

Vingerafdruk

enzymology
Enzymes
Signal-To-Noise Ratio
enzymes
Molecules
augmentation
Signal to noise ratio
molecules
signal to noise ratios
Confocal microscopy
Brownian movement
Electromagnetic Phenomena
Fluorescent Dyes
Photons
Confocal Microscopy
Catalytic Domain
products
acceleration (physics)
Fluorescence
Guidelines

Citeer dit

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title = "Plasmon-enhanced single-molecule enzymology",
abstract = "We present a numerical study on plasmon-enhanced single-molecule enzymology. We combine Brownian dynamics and electromagnetic simulations to calculate the enhancement of fluorescence signals of fluorogenic substrate converted by an enzyme conjugated to a plasmonic particle. We simulate the Brownian motion of a fluorescent product away from the active site of the enzyme, and calculate the photon detection rate taking into account modifications of the excitation and emission processes by coupling to the plasmon. We show that plasmon enhancement can boost the signal-to-noise ratio (SNR) of single turnovers by up to 100 fold compared to confocal microscopy. This enhancement factor is a trade-off between the reduced residence time in the near-field of the particle, and the enhanced emission intensity due to coupling to the plasmon. The enhancement depends on the size, shape and material of the particle and the photophysical properties of the fluorescent product. Our study provides guidelines on how to enhance the SNR of single-molecule enzyme studies and may aid in further understanding and quantifying static and dynamic heterogeneity.",
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Plasmon-enhanced single-molecule enzymology. / Wang, Yuyang; Zijlstra, Peter.

In: ACS Photonics, Vol. 5, Nr. 8, 23.05.2018, blz. 3073–3081.

Onderzoeksoutput: Bijdrage aan tijdschriftTijdschriftartikelAcademicpeer review

TY - JOUR

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AB - We present a numerical study on plasmon-enhanced single-molecule enzymology. We combine Brownian dynamics and electromagnetic simulations to calculate the enhancement of fluorescence signals of fluorogenic substrate converted by an enzyme conjugated to a plasmonic particle. We simulate the Brownian motion of a fluorescent product away from the active site of the enzyme, and calculate the photon detection rate taking into account modifications of the excitation and emission processes by coupling to the plasmon. We show that plasmon enhancement can boost the signal-to-noise ratio (SNR) of single turnovers by up to 100 fold compared to confocal microscopy. This enhancement factor is a trade-off between the reduced residence time in the near-field of the particle, and the enhanced emission intensity due to coupling to the plasmon. The enhancement depends on the size, shape and material of the particle and the photophysical properties of the fluorescent product. Our study provides guidelines on how to enhance the SNR of single-molecule enzyme studies and may aid in further understanding and quantifying static and dynamic heterogeneity.

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