Binding properties of a streptavidin layer formed on a biotinylated Langmuir-Schaefer film of unfolded protein

Taiji Furuno

研究成果: Article査読

抄録

A Langmuir monolayer of carbonic anhydrase (CA) unfolded at an air/water interface was transferred onto the hydrophobic surface of a silicon wafer by means of the Langmuir-Schaefer technique. The transferred CA film was biotinylated and was incubated in a streptavidin (SAv) solution to obtain a densely packed SAv layer by biotin-SAv linkage. Biotinylated proteins including ferritin, catalase, alcohol dehydrogenase, and carbonic anhydrase were incubated with the SAv layer and binding of these proteins was examined by atomic force microscopy. High-density binding of the biotinylated proteins was observed, whereas the amount of adsorbed non-biotinylated proteins was low or negligible. The SAv layer on the Langmuir-Schaefer film of unfolded protein could become a basic architecture for protein immobilization studies.

本文言語English
ページ(範囲)40-47
ページ数8
ジャーナルThin Solid Films
604
DOI
出版ステータスPublished - 2016 4月 1

ASJC Scopus subject areas

  • 電子材料、光学材料、および磁性材料
  • 材料化学
  • 金属および合金
  • 表面、皮膜および薄膜
  • 表面および界面

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