• DocumentCode
    2315321
  • Title

    Terahertz imaging for label-free protein detection

  • Author

    Ogawa, Y. ; Hayashi, S. ; Yoshida, H. ; Otani, C. ; Kawase, K.

  • Author_Institution
    Tohoku Univ., Sendai, Japan
  • fYear
    2009
  • fDate
    21-25 Sept. 2009
  • Firstpage
    1
  • Lastpage
    2
  • Abstract
    We demonstrate an imaging method combined a terahertz time-domain spectroscopy and an interference effect for label-free protein detection on a membrane filter. Biotin is linked to the membrane using poly ethylene glycol (PEG) or poly ethylene glycol methyl ether (MPEG) to prevent it from being washed off. Binding of the biotin with streptavidin is then observed by measuring the terahertz signal change due to the variation of the membrane refractive index. From result of competition binding experiments, it becomes clear that specific binding of antibody protein are detected by using this imaging method. This technique is used only to detect the existence of the binding. And the selectivity depends absolutely on specific ligand-protein interactions. This measurement principle is suitable to high throughput detection for drug discovery.
  • Keywords
    biological techniques; electromagnetic wave interference; molecular biophysics; polymers; proteins; terahertz wave imaging; terahertz wave spectra; antibody protein specific binding; biotin-streptavidin binding; drug discovery; high throughput detection; interference effect; label free protein detection; membrane filter; membrane refractive index variation; polyethyleneglycol methylether; terahertz imaging; terahertz time domain spectroscopy; Anti-freeze; Biomembranes; Interference; Optical imaging; Proteins; Refractive index; Spectroscopy; Submillimeter wave filters; Submillimeter wave measurements; Time domain analysis;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Infrared, Millimeter, and Terahertz Waves, 2009. IRMMW-THz 2009. 34th International Conference on
  • Conference_Location
    Busan
  • Print_ISBN
    978-1-4244-5416-7
  • Electronic_ISBN
    978-1-4244-5417-4
  • Type

    conf

  • DOI
    10.1109/ICIMW.2009.5324637
  • Filename
    5324637