Guest-binding behavior of peptide nanocapsules self-assembled from viral peptide fragments

Abstract

The binding behavior of guests (dyes and DNA) into peptide nanocapsules formed via self-assembly of a 24-mer b-annulus peptide fragment obtained from the capsid protein of the tomato bushy stunt virus is reported. The pH dependence of the f potential of the peptide nanocapsules indicates that the C-and N-termini are directed to the exterior and interior of the nanocapsules, respectively. Equilibrium dialysis experiments with dyes and the peptide nanocapsules at pH 7 showed that the peptide nanocapsules tend to bind anionic dyes. Binding of sodium 8-anilinonaphthalene-1-sulfonate and uranine into the peptide nanocapsules minimally affected the size of the nanocapsules, whereas binding of other anionic dyes resulted in the formation of precipitates. In addition, binding of Thioflavin T to the b-annulus peptide promoted disassembly of the nanocapsules. Complexation of the b-annulus peptide with M13 phage DNA formed a core-shell nanosphere in which the DNA was encapsulated in the peptide assembly.

Construction of Functional Biomaterials by Biomolecular Self-Assembly

“…65 These results suggest that the C-terminal is directed to the outer surface, whereas the N-terminal is directed to the interior of the artificial capsids, which corresponds to the terminal-direction of the natural TBSV capsid. Thus, it is suggested that the outer surface of the artificial viral capsid is zwitterionic and the inside is cationic at neutral pH; therefore, it is considered that anionic molecules can be encapsulated inside.…”

A zeolite as a tool for successful refolding of PEGylated proteins and their reassembly with tertiary structures

“…It is expected that the inclusions hardly leak from protein nanoparticles in blood circulation when the particles are used as drug carriers for hydrophilic compounds. Various protein nanoparticles have been developed as drug carriers, including virus‐like nanoparticles, ferritins, heat shock proteins, vault particles, and lumazine synthases …”

Biomolecular Self-assembling Systems for Multivalent Ligand Display

“…Moreover, we succeeded in the syntheses of C 3 -symmetric glutathione (64)(65)(66) It is known that TBSV, which was first revealed by X-ray crystallography in spherical viruses, possesses an interesting "dodecahedral internal skeleton" composed of a C 3 -symmetric β-annulus motif (49,68). We envisaged that the synthetic peptide fragment (24 amino acids) participating in the formation of the internal skeleton would self-assemble into virus-like nanocapsules ( The pH dependence of the surface ζ-potentials of the viruslike nanocapsules self-assembled from the β-annulus peptides suggest that the C-terminal is directed to the surface, while the Nterminal is directed to the interior of the peptide nanocapsules (70), which corresponds to the terminal-direction of the natural TBSV capsid (68). Accordingly, C-terminal modifications with any ligand may cause ligand display on the virus-like nanocapsules.…”