Dressing up artificial viral capsids self-assembled from C-terminal-modified β-annulus peptides

Abstract

A variety of chemical approaches for the rational design of artificial proteins and peptides have been developed in recent years for the construction of self-assembled nanocapsules. It was previously found that a synthetic 24-mer β-annulus peptide, which participates in the formation of the dodecahedral internal skeleton of the tomato bushy stunt virus capsid, spontaneously self-assembled into artificial viral capsids with a size of 30–50 nm. These artificial viral capsids were established to encapsulate various guest molecules, such as anionic dyes, DNA, quantum dots, and His-tagged proteins. The artificial viral capsids could also be dressed up with gold nanoparticles, single-stranded DNA, coiled-coil spikes, and proteins by modifying with these molecules at the C-terminus of β-annulus peptides. The artificial viral capsids were notably stabilized by dressing up with human serum albumin and acquired enzymatic activity by dressing up with ribonuclease. It was found that a synthetic 24-mer β-annulus peptide, which participates in the formation of the dodecahedral internal skeleton of the tomato bushy stunt virus capsid, spontaneously self-assembled into artificial viral capsids with a size of 30–50 nm. The artificial viral capsids could be dressed up with gold nanoparticles, single-stranded DNA, coiled-coil spikes, and proteins by modifying with these molecules at the C-terminus of β-annulus peptides. The artificial viral capsids were notably stabilized by dressing up with human serum albumin and acquired enzymatic activity by dressing up with ribonuclease.