Journal
NANO LETTERS
Volume 16, Issue 9, Pages 5944-5950Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.nanolett.6b02948
Keywords
Protein engineering; protein supramolecular structure; virus structure; bacteriophage MS2; drug delivery; nanocontainers
Categories
Funding
- National Science Foundation [MCB1150567]
- Army Research Office [W911NF-15-1-0144]
- ExxonMobil Corporation
- Hellman Family Faculty Fund
- UC Berkeley
- NDSEG Graduate Fellowship
- NIH [GM066698]
- National Institutes of Health, National Institute of General Medical Sciences
- Howard Hughes Medical Institute
- Office of Science, Office of Basic Energy Sciences, of the U.S. Department of Energy [DE-AC02-05CH11231]
- Direct For Biological Sciences [1150567] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience [1150567] Funding Source: National Science Foundation
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Virus-like particles are used to encapsulate drugs, imaging agents, enzymes, and other biologically active molecules in order to enhance their function. However, the size of most virus-like particles is inflexible, precluding the design of appropriately sized containers for different applications. Here, we describe a chromatographic selection for virus-like particle assembly. Using this selection, we identified a single amino acid substitution to the,coat protein of bacteriophage MS2 that mediates a uniform switch in particle geometry from T = 3 to T = 1 icosahedral symmetry. The resulting smaller particle retains the ability to be disassembled and reassembled in vitro and to be chemically modified to load cargo into its interior cavity. The pair of 27 and 17 nm MS2 particles will allow,direct examination of the effect of size on function in established applications of virus-like particles, including drug:delivery and imaging.
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