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Modular Virus Capsid Coatings for Biocatalytic DNA Origami Nanoreactors
Iris Seitz1, Donna McNeale1,2, Frank Sainsbury2
1Department of Bioproducts and Biosystems, Aalto University, Aalto 00076, Finland.
ACS Nano
|October 8, 2025
Summary
This study combines DNA origami and virus capsid proteins to create novel nanoreactors. These nanoreactors offer controlled enzyme loading, size-selective substrate uptake, and enhanced stability for biocatalysis and biomedical applications.
Area of Science:
- Biotechnology
- Nanotechnology
- Biochemistry
Background:
- Protein cages and DNA origami are self-assembling nanocompartments for enzyme sequestration.
- They mimic natural biocatalytic compartmentalization but face challenges in controlled enzyme loading and substrate flux.
- Combining these nanomaterials offers a potential solution to overcome these limitations.
Purpose of the Study:
- To develop a modular platform by assembling virus capsid proteins onto enzyme-loaded DNA origami nanoreactors.
- To investigate the impact of capsid protein properties on substrate uptake and enzyme protection.
- To explore the potential for targeted delivery via surface functionalization.
Main Methods:
- Assembly of virus capsid proteins onto enzyme-loaded DNA origami nanoreactors.
- Characterization of substrate uptake selectivity based on capsid protein type and amount.
- Assessment of enzyme protection against degradation.
- Functionalization of nanoreactor surfaces with antibody fragments.
Main Results:
- Demonstrated size-selective substrate uptake, modulated by capsid protein composition and quantity.
- Confirmed protection of the encapsulated biocatalytic unit from degradation.
- Successfully functionalized nanoreactor surfaces for potential targeting.
- Established a modular platform for investigating capsid protein properties.
Conclusions:
- The combined DNA origami and virus capsid protein approach creates a versatile nanoreactor platform.
- This platform enables controlled enzyme loading, selective substrate permeation, and enhanced stability.
- The modularity facilitates biomedical applications and research into capsid protein physicochemical properties.
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