Self-assembly of Ni-NTA-modified β-annulus peptides into artificial viral capsids and encapsulation of His-tagged proteins

Org Biomol Chem. 2016 Aug 16;14(33):7869-74. doi: 10.1039/c6ob01227b.

Abstract

β-Annulus peptides bearing Cys at the N-terminal from tomato bushy stunt virus were synthesised using a standard Fmoc-protected solid-phase method, and the peptide was modified with Ni-NTA at the N-terminal. The Ni-NTA-modified β-annulus peptide self-assembled into virus-like nanocapsules of approximately 40 nm in diameter. The critical aggregation concentration of these nanocapsules in 10 mM Tris-HCl buffer (pH 7.3) at 25 °C was 0.053 μM, which is 470 times lower than that of unmodified β-annulus peptides. Moreover, size exclusion chromatography of the peptide assembly indicated encapsulation of His-tagged green fluorescent protein in the Ni-NTA-modified artificial viral capsid.

MeSH terms

  • Capsid Proteins / chemistry*
  • Green Fluorescent Proteins / chemistry*
  • Histidine / chemistry*
  • Nickel / chemistry*
  • Nitrilotriacetic Acid / chemistry*
  • Peptides / chemical synthesis*
  • Peptides / chemistry

Substances

  • Capsid Proteins
  • Peptides
  • Green Fluorescent Proteins
  • Histidine
  • Nickel
  • Nitrilotriacetic Acid