In 2010, we found that the β-Annulus motif peptide (INHVGGTGGAIMAPVAVTRQLVGS) involved in the skeletal structure of tomato bushy stunt virus self-assembles in water to form an “artificial virus capsid” with about 30-50 nm diameter. Small-angle X-ray scattering has shown that this peptide assembly is a hollow structure, and the pH dependence of the ζ-potential indicates that the C-terminus of the peptide is oriented outward and the N-terminus inward. The N-terminal modification of the peptide can be used to encapsulate proteins, nucleic acids, and nanoparticles into artificial viral capsids. and is expected to be useful for various applications such as drug carriers. The C-terminal modification of the peptide enables the creation of artificial viral capsids modified with various functional molecules, which are expected to be useful for applications such as synthetic vaccines.

Representative papers

• Angew. Chem. Int. Ed., 49, 9662-9665 (2010).
• Polymer J., 45, 529-534 (2013).
• Nanomaterials, 4, 778-791 (2014).
• Polymer J., 47, 146-151 (2015).
• Org. Biomol. Chem., 14, 7869-7874 (2016).
• Chem. Lett., 45, 922-924 (2016).
• Org. Biomol. Chem., 15, 5070-5077 (2017). 
• J. Pept. Sci., 23, 636-643 (2017).
• Chem. Commun., 54, 8944-8959 (2018). Feature Article
• Bioconjug. Chem., 30, 1636-1641 (2019).
• Chem. Lett., 48, 544-546 (2019).
• Appl. Sci., 10, 8004 (2020).
• J. Org. Chem., 85, 1668-1673 (2020). 
• Bioconjug. Chem., 33, 311-320 (2022).
• ChemBioChem, 23, e202200220 (2022).
• Chem. Lett., 51, 1087-1090 (2022).
• J. Mater. Chem. B, 11, 6053–6059 (2023). Back Cover