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Updated: Jan 29, 2026

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
Encapsulation of fragmented cargo by virus coat proteins
Paul van der Schoot1, Roya Zandi2, Ayesha Amjad3
1Department of Applied Physics and Science Education, Eindhoven University of Technology, Postbus 513, 5600 MB Eindhoven, The Netherlands.
Nanoparticle and virus coat protein co-assembly is sensitive to size and ratio. A mass-action model explains why larger nanoparticles are preferred and capsids are not fully filled due to entropy.
Area of Science:
- Biophysics
- Materials Science
- Nanotechnology
Background:
- Co-assembly of nanoparticles and virus coat proteins is crucial for nanotechnology applications.
- Experimental studies show sensitivity to nanocolloid size and nanoparticle-to-protein ratio.
- Larger nanoparticles are preferentially encapsulated in competitive scenarios.
Purpose of the Study:
- To rationalize experimental findings on nanoparticle-virus coat protein co-assembly.
- To investigate the influence of nanoparticle size and stoichiometry on capsid formation.
- To understand the factors governing nanoparticle encapsulation within viral capsids.
Main Methods:
- Development of a simple mass-action model.
- Inclusion of free nanoparticles, coat proteins, and various complex formations.
- Analysis of equilibrium between different molecular species.
Main Results:
- A narrow range of nanocolloid concentrations permits significant partially filled capsid formation.
- The number of encapsulated nanoparticles is typically less than the maximum wall capacity.
- Entropy's impact offsets binding free energy gains, particularly for smaller nanoparticles.
Conclusions:
- The mass-action model qualitatively agrees with experimental observations.
- Entropic effects play a significant role in limiting nanoparticle encapsulation.
- Understanding these principles is key for designing controlled nanoparticle-protein co-assembly systems.
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