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Common-path phase-shift interferometry surface plasmon resonance imaging system.

Y D Su1, S J Chen, T L Yeh

  • 1Department of Engineering Science, National Cheng Kung University, Tainan 701, Taiwan.

Optics Letters
|July 13, 2005
PubMed
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This study integrates Surface Plasmon Resonance (SPR) and Phase-Shift Interferometry (PSI) for label-free biosensing. The novel SPR-PSI system achieves high sensitivity and stability for real-time biomolecular interaction analysis.

Area of Science:

  • Biophotonics
  • Biosensing Technology
  • Surface Plasmon Resonance Imaging

Background:

  • Label-free detection of biomolecular interactions is crucial for real-time kinetic studies.
  • Traditional biosensing methods may require additional labeling, complicating analysis.
  • Common-path Phase-Shift Interferometry (PSI) offers excellent long-term stability against disturbances.

Purpose of the Study:

  • To develop and demonstrate an integrated Surface Plasmon Resonance (SPR) and PSI biosensing imaging system.
  • To enable label-free, real-time measurement of 2D spatial phase variations from biomolecular interactions.
  • To assess the system's sensitivity, stability, and spatial resolution.

Main Methods:

  • Integration of Surface Plasmon Resonance (SPR) with common-path Phase-Shift Interferometry (PSI).

Related Experiment Videos

  • Development of a biosensing imaging system for label-free biomolecular interaction analysis.
  • Utilizing 2D spatial phase variation measurement on a sensing chip.
  • Main Results:

    • Achieved a detection limit of 2 x 10(-7) refractive-index change.
    • Demonstrated long-term phase stability of 2.5 x 10(-4) pi rms over 4 hours.
    • Obtained a spatial phase resolution of 10(-3) pi with 100 microm lateral resolution.

    Conclusions:

    • The integrated SPR-PSI system provides a sensitive and stable platform for label-free biosensing.
    • The system is suitable for real-time kinetic studies of biomolecular interactions.
    • High spatial and phase resolution enables detailed analysis of binding events.