Analysis of biomolecular interactions using a miniaturized surface plasmon resonance sensor

Area of Science:

• Biophotonics
• Biosensing Technology
• Analytical Chemistry

Background:

• Miniaturized sensors are crucial for advancing bioanalytical applications.
• Surface Plasmon Resonance (SPR) offers label-free detection of biomolecular interactions.
• Evaluating commercial SPR devices is essential for practical implementation.

Purpose of the Study:

• To assess the performance of a commercially available miniaturized SPR sensor for biological interaction analysis.
• To determine the sensor's repeatability, linearity, and reproducibility.
• To explore surface immobilization techniques and validate measurements against established methods.

Main Methods:

• Utilized a commercial miniaturized SPR sensor.
• Tested sensor performance with high-refractive index solutions and protein binding.
• Employed biotin/avidin and glycoprotein/lectin chemistries for surface immobilization.
• Determined equilibrium dissociation constants (KD) for specific biomolecular interactions.
• Validated results using surface fluorescence microscopy and fluorescence correlation spectroscopy.

Main Results:

• The SPR sensor demonstrated excellent repeatability and linearity for high-refractive index solutions.
• Good reproducibility was observed for protein binding assays.
• Achieved a detection limit of 2.1 fmol for monoclonal antibody M1 (21 pg/mm2).
• Equilibrium dissociation constants determined by SPR closely agreed with other methods.
• Successful exploration of simple surface immobilization strategies.

Conclusions:

• The miniaturized SPR sensor is a reliable and accurate tool for bioanalytical applications.
• Its performance characteristics make it suitable for both laboratory and clinical settings.
• The sensor represents an inexpensive, portable, and effective solution for biomolecular interaction analysis.