論文

査読有り
2015年3月1日

SV40 VP1 major capsid protein in its self-assembled form allows VP1 pentamers to coat various types of artificial beads in vitro regardless of their sizes and shapes

Biotechnology Reports
  • Masaaki Kawano
  • Koji Doi
  • Hajime Fukuda
  • Yoshinori Kita
  • Kensuke Imai
  • Takamasa Inoue
  • Teruya Enomoto
  • Masanori Matsui
  • Mamoru Hatakeyama
  • Yuki Yamaguchi
  • Hiroshi Handa
  • 全て表示

5
1
開始ページ
105
終了ページ
111
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.btre.2014.12.008
出版者・発行元
Elsevier B.V.

The icosahedral capsid structure of simian virus 40 (diameter, 45nm) consists of 72 pentameric subunits, with each subunit formed by five VP1 molecules. Electron microscopy, immuno-gold labeling, and ζ-potential analysis showed that purified recombinant VP1 pentamers covered polystyrene beads measuring 100, 200, and 500nm in diameter, as well as silica beads. In addition to covering spherical beads, VP1 pentamers covered cubic magnetite beads, as well as the distorted surface structures of liposomes. These findings indicate that VP1 pentamers could coat artificial beads of various shapes and sizes larger than the natural capsid. Technology based on VP1 pentamers may be useful in providing a capsid-like surface for enclosed materials, enhancing their stability and cellular uptake for drug delivery systems.

リンク情報
DOI
https://doi.org/10.1016/j.btre.2014.12.008
ID情報
  • DOI : 10.1016/j.btre.2014.12.008
  • ISSN : 2215-017X
  • SCOPUS ID : 84926320553

エクスポート
BibTeX RIS