Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 61, Issue 2, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202111687
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Funding
- Defense Threat Reduction Agency [HDTRA11810029]
- National Institutes of Health [1R01 AI139748]
- U.S. Department of Defense (DOD) [HDTRA11810029] Funding Source: U.S. Department of Defense (DOD)
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This study identified a simple general method for non-covalent packaging and subsequent release of functional molecules inside nucleoprotein nanocages, independent of modifications to the capsid protein.
Virus-like particles (VLPs) derived from Leviviridae virions contain substantial amounts of cellular and plasmid-derived RNA. This encapsidated polynucleotide serves as a reservoir for the efficient binding of the intercalating dye thiazole orange (TO). Polyethylene glycol (PEG) molecules and oligopeptides of varying length, end-functionalized with TO, were loaded into VLPs up to approximately 50% of the mass of the capsid protein (hundreds to thousands of cargo molecules per particle, depending on size). The kinetics of TO-PEG binding included a significant entropic cost for the reptation of long chains through the capsid pores. Cargo molecules were released over periods of 20-120 hours following simple reversible first-order kinetics in most cases. These observations define a simple general method for the non-covalent packaging, and subsequent release, of functional molecules inside nucleoprotein nanocages in a manner independent of modifications to the capsid protein.
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