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Determination of the Excitation and Coupling Rates Between Light Emitters and Surface Plasmon Polaritons
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Development of surface plasmon resonance mass spectrometry array platform.

Dobrin Nedelkov1

  • 1Intrinsic Bioprobes Inc., 2155 East Conference Drive, Suite 104 Tempe, Arizona 85284, USA. dnedelkov@intrinsicbio.com

Analytical Chemistry
|June 26, 2007
PubMed
Summary

This study introduces a novel dual detection method combining surface plasmon resonance (SPR) and mass spectrometry (MS) for protein microarrays. This SPR-MS approach enables comprehensive protein analysis on a single high-content chip.

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Area of Science:

  • Biotechnology
  • Analytical Chemistry
  • Proteomics

Background:

  • Protein microarrays are crucial for high-throughput protein interaction analysis.
  • Current methods often rely on multistep reporter molecule detection.
  • Label-free detection methods like SPR and MS show promise but are underutilized in high-content arrays.

Purpose of the Study:

  • To demonstrate the first combined surface plasmon resonance (SPR) and mass spectrometry (MS) detection on a single high-content protein microarray.
  • To evaluate the utility of this dual SPR-MS approach for comprehensive protein analysis.

Main Methods:

  • Antibodies for five human plasma proteins were arrayed on a gold-coated glass chip.
  • Surface plasmon resonance imaging (SPRi) was used for real-time binding monitoring.
  • Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) was applied post-binding for mass analysis.

Main Results:

  • SPR imaging successfully monitored protein binding across the entire microarray surface.
  • MALDI-MS analysis generated protein-specific mass spectra from distinct array spots.
  • The SPR-MS dual detection successfully identified bound proteins.

Conclusions:

  • The combined SPR-MS detection is highly suitable for high-content protein microarrays.
  • This method allows for quantitative assessment of protein concentration.
  • It also facilitates the detection of structural protein variants, including those from genetic variations and post-translational modifications.