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

Fingerprint

Streptavidin
Langmuir Blodgett films
Carbonic anhydrase
Carbonic Anhydrases
carbonic anhydrase
proteins
Proteins
Alcohol Dehydrogenase
catalase
Ferritins
Biotin
biotin
Silicon wafers
dehydrogenases
monomolecular films
Catalase
Monolayers
Atomic force microscopy
immobilization
Carrier Proteins

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

Cite this

Binding properties of a streptavidin layer formed on a biotinylated Langmuir-Schaefer film of unfolded protein. / Furuno, Taiji.

In: Thin Solid Films, Vol. 604, 01.04.2016, p. 40-47.

Research output: Contribution to journalArticle

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