@article{oai:repository.lib.tottori-u.ac.jp:00007320,
 author = {Matsuura, Kazunori and Matsuura, Kazunori and Nakamura, Tomohiro and Watanabe, Kenta and Noguchi, Takanori and Minamihata, Kosuke and Kamiya, Noriho and Kimizuka, Nobuo and Nakamura, Tomohiro and Watanabe, Kenta and Noguchi, Takanori and Minamihata, Kosuke and Kamiya, Noriho and Kimizuka, Nobuo},
 issue = {33},
 journal = {Organic & biomolecular chemistry, Organic & biomolecular chemistry},
 month = {},
 note = {β-Annulus peptide bearing Cys at the N-terminal from tomato bushy stunt virus was synthesised using a standard Fmoc-protected solid-phase method, and the petide 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.},
 pages = {7869--7874},
 title = {Self-assembly of Ni-NTA-modified β-Annulus Peptides into Artificial Viral Capsids and Encapsulation of His-tagged Proteins},
 volume = {14},
 year = {2016}
}