Jump to main content
Jump to site search

Issue 33, 2016
Previous Article Next Article

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

Author affiliations

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.

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

Back to tab navigation

Publication details

The article was received on 06 Jun 2016, accepted on 04 Jul 2016 and first published on 04 Jul 2016


Article type: Paper
DOI: 10.1039/C6OB01227B
Citation: Org. Biomol. Chem., 2016,14, 7869-7874
  •   Request permissions

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

    K. Matsuura, T. Nakamura, K. Watanabe, T. Noguchi, K. Minamihata, N. Kamiya and N. Kimizuka, Org. Biomol. Chem., 2016, 14, 7869
    DOI: 10.1039/C6OB01227B

Search articles by author

Spotlight

Advertisements