Self-assembled artificial viral capsids bearing coiled-coils at the surface

Abstract

In order to construct artificial viral capsids bearing complementary dimeric coiled-coils on the surface, a β-annulus peptide bearing a coiled-coil forming sequence at the C-terminus (β-annulus-coiled-coil-B) was synthesized by a native chemical ligation of a β-annulus-SBn peptide with a Cys-containing coiled-coil-B peptide. Dynamic light scattering (DLS) measurements and transmission electron microscopy (TEM) images revealed that the β-annulus-coiled-coil-B peptide self-assembled into spherical structures of about 50 nm in 10 mM Tris-HCl buffer. Circular dichroism (CD) spectra indicated the formation of the complementary coiled-coil structure on the spherical assemblies. Addition of 0.25 equivalent of the complementary coiled-coil-A peptide to the β-annulus-coiled-coil-B peptide showed the formation of spherical assemblies of 46 ± 14 nm with grains of 5 nm at the surface, whereas addition of 1 equivalent of the complementary coiled-coil-A peptide generated fibrous assemblies.

Peptide-induced super-assembly of biocatalytic metal–organic frameworks for programmed enzyme cascades

“…Among them, helical hetero-dimers have wide applications in the design of three-dimensional (3D) nanostructures. For example, complementary dimeric coiled-coil peptides can induce the self-assembly of artificial viral capsids 40,41. Protein–protein helical hetero-dimers were used in colloidal assembly of polystyrene microparticles42 and protein super-structures 43.…”

Tetramerizing tGCN4 domain facilitates production of Influenza A H1N1 M2e higher order soluble oligomers that show enhanced immunogenicity in vivo

“…CD analysis has shown that both the mammalian and bacterial expressed proteins are structurally stable, although the molar ellipticity per residue for the bacterial express protein is lower compared to the M1-2x and M2-3x proteins. It is to be noted that both M1-2x and M2-3x have the tGCN4 tetramerization domain that forms highly coiled-coil leucine zipper, tetramer structure that is rich in alpha-helix that significantly contributed for the high molar ellipticity in the tGCN4 tagged proteins and the spectra generated might be coming from the tGCN4 domains (67).…”

Multivalent display of chemical signals on self‐assembled peptide scaffolds

“…Typically, assembly motifs that are effective for the display of high molecular weight functional motifs are also folded proteins such as those that comprise viral capsids. [203,204] The resulting supramolecular structures thus tend to be three-dimensional capsids or particles that maximize the spatial separation of the large displayed cargo. For example, Matsuura et al [67] have engineered a system that displays human serum albumin (HSA) on a viral capsid mimetic ( Figure 3).…”