Light Undergoing Total Internal Reflection

Surface Plasmon Resonant Angle

Applications Surface Plasmon Resonance

How does SPR work?

Applications of SPR

Examples of molecular binding events

Binding kinetics

Binding Affinity

Why do Metals reflect?

What is Plasma?

How can plasma be generated?

Applications of plasma

Why Plasma?

What happens during reflection?

Incident Electromagnetic Wave

Generation of Electromagnetic waves

Non-Ideal metals

Surface Plasmon Resonance

Intro

What is SPR?

Ligand and analyte

Optical detection system

Intensity versus angle

Monitoring binding events

Measuring Binding Responses

Binding Response

Equilibrium

Conclusion

Surface Plasmon Resonance or SPR for short is an optical technology used to perform label-free biomolecular interaction analysis in real-time.

This fluidic-based design uses sensor chips which are addressed with the sample through a microfluidic system for a wide range of molecules.

SPR occurs when light moves from an optically dense medium to a less dense medium, such as from glass to air. It moves away from normal, and at an angle greater than the critical angle, it undergoes total internal reflection.

If a thin gold layer is placed on at the interface, then some of the reflected light is absorbed, reducing the intensity of reflected light at a specific angle known as the resonance angle.

This localization of these plasmons to the boundary and external medium makes surface plasmon resonance highly sensitive to any changes that occur within the field of the plasmon wave. Therefore, any change in the refractive index will result in a change of the SPR angle.

When a sample containing an analyte of interest is injected over the sensor chip, any binding of the analyte to immobilized ligands on the chip causes a change in the refractive index at the surface, …

resulting in a shift in the angle of total reflected light.

This shift can be monitored and plotted in real-time and is directly proportional to the amount of binding that occurs, …

allowing researchers to quantify the binding kinetics and affinity of the biomolecular interaction.

Throughput, flexibility, and sensitivity of the SPR platform gives researchers the potential to characterize biomolecular interactions in any binding study.

A wide range of molecules can be studied, from ions, fragments and small molecules to proteins and viruses.

Label-free biomolecular interaction analysis has revolutionized the field of antibody discovery and development. It has enabled researchers to assess the binding characteristics of potential therapeutic antibodies quickly and accurately - ultimately leading to significant advances in the development of such for more effective and specific biotherapeutics.

Sartorius – Simplifying Progress