prc8(11)_pr8111455.pdf 3.21 MB
松浦 和則 Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University / Centre for Research on Green Sustainable Chemistry, Tottori University 研究者総覧 KAKEN
Shiomi, Yuriko Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University
Mizuta, Toshihumi Technical Department, Tottori University
artificial viral capsid
Artificial construction of spherical protein assemblies has attracted considerable attention due to its potential use in nanocontainers, nanocarriers, and nanoreactors. In this work, we demonstrate a novel strategy to construct peptide nanocapsules (artificial viral capsids) decorated with enzymes via interactions between His-tag and Ni-NTA. A β-annulus peptide derived from the tomato bushy stunt virus was modified with Ni-NTA at the C-terminus, which is directed toward the exterior surface of the artificial viral capsid. The β-annulus peptide bearing Ni-NTA at the C-terminus self-assembled into capsids of about 50 nm in diameter. The Ni-NTA-displayed capsids were complexed with recombinant horseradish peroxidase (HRP) with a C-terminal His-tag which was expressed in Escherichia coli. The β-annulus peptide-HRP complex formed spherical assemblies whose sizes were 30–90 nm, with the ζ-potential revealing that the HRP was decorated on the outer surface of the capsid.
(C) 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
Matsuura Kazunori, Shiomi Yuriko, Mizuta Toshihumi, et al. Horseradish Peroxidase-Decorated Artificial Viral Capsid Constructed from β-Annulus Peptide via Interaction between His-Tag and Ni-NTA. PROCESSES. 2020. 8(11). doi:10.3390/pr8111455
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