Biomolecular Interaction Characterization

The most popular use of Surface Plasmon Resonance is in the study of biomolecular interactions.  The wide dynamic range of SPR enables it to be used to analyze a wide variety of interactions:

Protein-Protein

Interactions between large molecules e.g., Antibody Antigen are common studies using SPR. For this type of experiment, a minimal amount of one of the proteins is coupled to get good kinetics.  For more information on this type of experiment, see the following Application Notes:

  1. Biotinylated HSA/Anti HSA Binding
  2. SPR Capture Analysis
  3. Capture vs. Coupling of Antibody
  4. High-throughput Antibody-Antigen Analysis
  5. Small Volume Injections

Protein-Small Molecule

This type of interaction usually involves the immobilization of the large molecule and creation of a high density surface, especially if the weight difference is very large.  Small molecules studied with SPR can have molecular weights of 100 Da or less.  For more information, see the following Application Notes:

  1. Small Molecule Binding
  2. Small Molecule Binding Reproducibility

Protein-DNA

This type of experiment is typically carried out by capturing biotinylated DNA over a streptavidin surface.  For a recent example where a Reichert SPR was used for this type of experiment, see the following publication: Kevin E. Siters, Stephanie A. Sander, Jason R. Devlin, and Janet R. Morrow. "Bifunctional Zn (ii) complexes for recognition of non-canonical thymines in DNA bulges and G-quadruplexes." Dalton Transactions, 2015, 44, 3708-3716.

1. DNA Binding to Zinc Complexes