Self-assembly of Ni-NTA-modified β-annulus peptides into artificial viral capsids and encapsulation of His-tagged proteins. Issue 33 (8th July 2016)

• Record Type: Journal Article
• Authors: Matsuura, Kazunori; Nakamura, Tomohiro; Watanabe, Kenta; Noguchi, Takanori; Minamihata, Kosuke; Kamiya, Noriho; Kimizuka, Nobuo
• Is Part Of: Organic & biomolecular chemistry. Volume 14:Issue 33(2016)
• Page Start: 7869
• Page End: 7874
• Publication Date: 2016-07-08
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c6ob01227b
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : His-tagged proteins were encapsulated into artificial viral capsids self-assembled from Ni-NTA-modified β-annulus peptides. 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.