CreMap™ Epitope Mapping by Surface Plasmon Resonance

Creative Biolabs helps to figure out epitopes by providing mapping services with Surface Plasmon Resonance (SPR) technology that is quite useful in the evaluation of antigen-antibody interaction, affinity measurement, competition assays, ligand fishing, ADME (adsorption, distribution, metabolism, and excretion) characterization.

SPR is the resonant oscillation of conduction electrons at the interface between negative and positive permittivity material stimulated by incident light. SPR allows for the analysis of the association and dissociation rate constants and modeling of biomolecular interaction kinetics. For epitope mapping analysis, the antigen is typically immobilized on a sensor chip surface, and the antibody flows through a microfluidic system in contact with the chip surface. SPR measures in real time the changes in mass bound to the sensor chip. It detects the changes in refractive index of the surface layer of a solution in contact with the sensor chip that is caused by a variation of the mass on the sensor chip surface. SPR immunoassay resembles the concept of the ELISA technique, but it is label-free, eliminating the requirement for reporter molecules or tags which could be time-consuming and even alter the molecular interaction.

CreMap™ Epitope Mapping by Surface Plasmon Resonance
Fig.1 The schematic of the surface plasmon resonance measurement.

Method

Surface plasmon resonance (SPR) is a label-free optical sensing technique to characterize binding between a soluble ligand and a surface-immobilized receptor.

The antigen is immobilized on the surface of the sensor chip.
The antibody flows through the microfluidic system.
The antibody binds the candidate antigen at the interface causing an increase in refractive index, which results in a shift in resonance angle and a change in the SPR signal.
SPR signal changes as a function of time are collected by the detector and allow the calculation of association (k_a) and dissociation (k_d) rate constants.
k_a and k_d constants are used to determine affinity and epitopes.

Key Features

Label-free: one of the main features of SPR used for epitope mapping is that SPR detects the interaction between the antigen and antibody with no labels.
Low purity requirement: the purified sample is ideal for identification, but purified samples are not always available. SPR can be applied to test crude samples, reducing the time and cost spent on purifying samples. SPR stands out as one of the best options when the antigen purification is not possible.
Small amounts of reagents required: only a small amount of samples are required for SPR to run the epitope mapping analysis, reducing the cost of expensive materials and making SPR more affordable.

SPR is a powerful method for characterizing the epitopes on the antigen.Scientists from Creative Biolabs have been working on developing and optimizing our SPR platform to better serve growing demands of customers around the world. If you are trying to figure out epitopes on the antigen, or if you are interested in our platform, please feel free tocontact us by sending E-mail. A formal feedback will be sent back as soon as possible.

References

Wittenberg, N.J., et al., Applications of SPR for the characterization of molecules important in the pathogenesis and treatment of neurodegenerative diseases. Expert Rev Neurother, 2014. 14(4): p. 449-63.
Cooper, M.A., Optical biosensors in drug discovery. Nat Rev Drug Discov, 2002. 1(7): p. 515-28.
Stahelin, R.V., Surface plasmon resonance: a useful technique for cell biologists to characterize biomolecular interactions. Mol Biol Cell, 2013. 24(7): p. 883-6.
Myszka, D.G., Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Curr Opin Biotechnol, 1997. 8(1): p. 50-7.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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