Development of the myoglobin sensor based on the surface plasmon resonance

Area of Science:

• Biomedical Engineering
• Biosensor Technology
• Analytical Chemistry

Background:

• Surface Plasmon Resonance (SPR) is a label-free optical technique widely used for detecting biomolecular interactions.
• Antigen-antibody (Ag-Ab) interactions are crucial in diagnostics and biological research, requiring sensitive and rapid detection methods.
• Developing efficient bioaffinic sensors is essential for precise control and monitoring of these interactions.

Purpose of the Study:

• To develop and characterize a novel bioaffinic sensor for detecting antigen-antibody interactions.
• To evaluate the sensor's sensitivity and performance in quantifying antibodies against human heart myoglobin.
• To assess the reusability and dynamic properties of the developed biosensor.

Main Methods:

• Fabrication of a bioaffinic sensor using a gold layer as a transducer for Surface Plasmon Resonance (SPR) detection.
• Modification of the transducer surface with spontaneously organized molecular assemblies of mercaptans.
• Immobilization of human heart myoglobin onto the sensor surface for antibody capture.

Main Results:

• The developed SPR-based bioaffinic sensor successfully detected minimal concentrations of antibodies, as low as 1 ng/ml.
• The sensor demonstrated the ability to observe the dynamics of protein interactions with short incubation times (≤5 minutes).
• The biosensor maintained its performance over 7-9 cycles after specific binding was disrupted, indicating reusability.

Conclusions:

• The created bioaffinic sensor offers high sensitivity for detecting antibodies to human heart myoglobin.
• The sensor provides a rapid and reusable platform for monitoring antigen-antibody interactions.
• This technology holds potential for applications in diagnostics and biomedical research requiring sensitive biomolecular detection.