Time-resolved fluorescence anisotropy of labeled plasma proteins adsorbed on polymer surfaces

Hiroshi Fukumura, Kazuko Hayashi

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


The rotational motion of a pyrene sulfonyl group covalently bonded to plasma proteins was studied at the solution/polymer interface by a technique combining total internal reflection (TIR) with time-resolved fluorescence anisotropy. Assuming the time dependence of fluorescence anisotropy to be one exponential decay, the rotational correlation time (φ) was obtained. The values of φ varied with the polymer surfaces, whose hydrophobicities differ. It was presumed that the adsorbed proteins change conformation or orient particularly as if the fragmental motion of the protein molecules became dominant, in addition the interference of the protein rotation due to the surface adhesion.

Original languageEnglish
Pages (from-to)435-442
Number of pages8
JournalJournal of Colloid And Interface Science
Issue number2
Publication statusPublished - 1990 Mar 15

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Biomaterials
  • Surfaces, Coatings and Films
  • Colloid and Surface Chemistry


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