A robust and general approach to quantitatively conjugate enzymes to plasmonic nanoparticles

Yuyang Wang, Karsten van Asdonk, Peter Zijlstra (Corresponding author)

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Abstract

Bioconjugates of plasmonic nanoparticles have received considerable attention due to their potential biomedical applications. Successful bioconjugation requires control over the number and activity of the conjugated proteins and the colloidal stability of the particles. In practice, this requires reoptimization of the conjugation protocol for each combination of protein and nanoparticle. Here, we report a robust and general protocol that allows for the conjugation of a range of proteins to different types of nanoparticles using very short polyethylene-glycol(PEG) linkers, while simultaneously preserving protein activity and colloidal stability. The use of short linkers ensures that the protein is located close to the particle surface, where the refractive index sensitivity and near-field enhancement are maximal. We demonstrate that the use of a Tween20 containing stabilizing buffer is critical in maintaining colloidal stability and protein function throughout the protocol. We obtain quantitative control over the average number of enzymes per particle by either varying the number of functional groups on the particle or the enzyme concentration during incubation. This new route of preparing quantitative protein-nanoparticle bioconjugates paves the way to develop rational and quantitative strategies to functionalize nanoparticles for applications in sensing, medical diagnostics, and drug delivery.

Original languageEnglish
Pages (from-to)13356−13363
Number of pages8
JournalLangmuir
Volume35
Issue number41
DOIs
Publication statusPublished - 23 Sep 2019

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enzymes
Enzymes
Nanoparticles
proteins
Proteins
nanoparticles
conjugation
Drug delivery
preserving
Functional groups
Polyethylene glycols
glycols
polyethylenes
Refractive index
delivery
near fields
Buffers
drugs
buffers
routes

Cite this

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abstract = "Bioconjugates of plasmonic nanoparticles have received considerable attention due to their potential biomedical applications. Successful bioconjugation requires control over the number and activity of the conjugated proteins and the colloidal stability of the particles. In practice, this requires reoptimization of the conjugation protocol for each combination of protein and nanoparticle. Here, we report a robust and general protocol that allows for the conjugation of a range of proteins to different types of nanoparticles using very short polyethylene-glycol(PEG) linkers, while simultaneously preserving protein activity and colloidal stability. The use of short linkers ensures that the protein is located close to the particle surface, where the refractive index sensitivity and near-field enhancement are maximal. We demonstrate that the use of a Tween20 containing stabilizing buffer is critical in maintaining colloidal stability and protein function throughout the protocol. We obtain quantitative control over the average number of enzymes per particle by either varying the number of functional groups on the particle or the enzyme concentration during incubation. This new route of preparing quantitative protein-nanoparticle bioconjugates paves the way to develop rational and quantitative strategies to functionalize nanoparticles for applications in sensing, medical diagnostics, and drug delivery.",
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A robust and general approach to quantitatively conjugate enzymes to plasmonic nanoparticles. / Wang, Yuyang; van Asdonk, Karsten; Zijlstra, Peter (Corresponding author).

In: Langmuir, Vol. 35, No. 41, 23.09.2019, p. 13356−13363.

Research output: Contribution to journalArticleAcademicpeer-review

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