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

Taiji Furuno

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
Pages (from-to)40-47
Number of pages8
JournalThin Solid Films
Volume604
DOIs
Publication statusPublished - 2016 Apr 1

Keywords

  • Air/water interface
  • Biotinylation
  • Langmuir film
  • Langmuir-Schaefer film
  • Protein array
  • Protein monolayer
  • Streptavidin
  • Unfolding

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Materials Chemistry
  • Metals and Alloys
  • Surfaces, Coatings and Films
  • Surfaces and Interfaces

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