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Visualizing Diffusional Dynamics of Gold Nanorods on Cell Membrane using Single Nanoparticle Darkfield Microscopy
Published on: March 5, 2021
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Study Enhanced Enzyme Diffusion with High-Speed Single Nanoparticle Rotational and Translational Tracking
Xijian Lin1, Yan He1
1Department of Chemistry, Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education), Tsinghua University, Beijing 100084, China.
Analytical Chemistry
|May 9, 2022
Summary
Enzymatic reactions can cause localized environmental changes. This study used gold nanorods to reveal that active urease enzymes create inhomogeneous distributions in solution, affecting particle motion.
Area of Science:
- Biochemistry
- Physical Chemistry
- Nanotechnology
Background:
- Catalytic enzymes with enhanced motion are of significant interest.
- However, the environmental impact of enzyme activity remains poorly understood.
Purpose of the Study:
- To investigate the environmental effects of active enzymes using a model urease system.
- To simultaneously monitor the diffusion of single anisotropic gold nanorods (AuNRs) to probe these effects.
Main Methods:
- Utilized high-speed dark-field imaging to track the diffusion of individual AuNRs.
- Applied the Stokes-Einstein equation to analyze diffusion coefficients and infer environmental changes.
- Varied substrate concentration to observe effects on AuNR diffusion heterogeneity.
Main Results:
- Observed enhanced translational and rotational diffusion of AuNRs, with inconsistent degrees.
- Found increased spatial but decreased temporal heterogeneity in AuNR diffusion with rising substrate concentration.
- Detected intermittent ballistic motion in AuNRs, suggesting localized environmental disturbances.
Conclusions:
- The catalytic reaction of urease induces localized, inhomogeneous distributions of enzymes in solution.
- These enzymatic reactions subtly affect the local physicochemical environment, influencing particle dynamics.
- High-speed imaging of nanorods provides a sensitive method for studying enzyme-induced environmental heterogeneity.
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