Virus-like particles (VLPs) derived from Leviviridae virions contain substantial amounts of cellular and plasmid-derived RNA. This encapsidated polynucleotide serves as areservoir 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 as ignificant entropic cost for the reptation of long chains through the capsid pores.C argo molecules were released over periods of 20-120 hours following simple reversible first-order kinetics in most cases.T hese observations define as imple general method for the noncovalent packaging,a nd subsequent release,o ff unctional molecules inside nucleoprotein nanocages in am anner 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 areservoir 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 as ignificant entropic cost for the reptation of long chains through the capsid pores.C argo molecules were released over periods of 20-120 hours following simple reversible first-order kinetics in most cases.T hese observations define as imple general method for the noncovalent packaging,a nd subsequent release,o ff unctional molecules inside nucleoprotein nanocages in am anner independent of modifications to the capsid protein.