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Title: Cargo Retention inside P22 Virus-Like Particles

Journal Article · · Biomacromolecules
 [1];  [1];  [2]; ORCiD logo [3];  [1];  [4]; ORCiD logo [1]
  1. Indiana Univ., Bloomington, IN (United States)
  2. Centro Nacional de Biotecnología (CNB-CSIC), Madrid (Spain); Centro Nacional de Microbiología/ISCIII, Madrid (Spain)
  3. Argonne National Lab. (ANL), Argonne, IL (United States)
  4. 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 Lab. (ANL), Argonne, IL (United States)
Sponsoring Organization:
USDOE Office of Science (SC); National Science Foundation (NSF); Spanish Ministerio de Economia y Competitividad (MINECO)
Grant/Contract Number:
AC02-06CH11357
OSTI ID:
1488561
Journal Information:
Biomacromolecules, Vol. 19, Issue 9; ISSN 1525-7797
Publisher:
American Chemical SocietyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 20 works
Citation information provided by
Web of Science

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Cited By (1)