Cargo Retention inside P22 Virus-Like Particles
Journal Article
·
· Biomacromolecules
- Indiana Univ., Bloomington, IN (United States)
- Centro Nacional de Biotecnología (CNB-CSIC), Madrid (Spain); Centro Nacional de Microbiología/ISCIII, Madrid (Spain)
- Argonne National Lab. (ANL), Argonne, IL (United States)
- Centro Nacional de Biotecnología (CNB-CSIC), Madrid (Spain)
We report that viral protein cages, with their regular and programmable architectures, are excellent platforms for the development of functional nanomaterials. The ability to transform a virus into a material with intended structure and function relies on the existence of a well-understood model system, a noninfectious virus-like particle (VLP) counterpart. Here, we study the factors important to the ability of P22 VLP to retain or release various protein cargo molecules depending on the nature of the cargo, the capsid morphology, and the environmental conditions. Because the interaction between the internalized scaffold protein (SP) and the capsid coat protein (CP) is noncovalent, we have studied the efficiency with which a range of SP variants can dissociate from the interior of different P22 VLP morphologies and exit by traversing the porous capsid. Finally, understanding the types of cargos that are either retained or released from the P22 VLP will aid in the rational design of functional nanomaterials.
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- National Science Foundation (NSF); Spanish Ministerio de Economia y Competitividad (MINECO); USDOE Office of Science (SC)
- Grant/Contract Number:
- AC02-06CH11357
- OSTI ID:
- 1488561
- Journal Information:
- Biomacromolecules, Journal Name: Biomacromolecules Journal Issue: 9 Vol. 19; ISSN 1525-7797
- Publisher:
- American Chemical SocietyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Structural nanotechnology: three-dimensional cryo-EM and its use in the development of nanoplatforms for in vitro catalysis
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journal | January 2019 |
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