Biomolecular interaction analysis seeks to understand the interactions between biomolecules and the results of these interactions. This type of analysis is critical for medical research and pharmaceuticals. Here we explain some of the key principles of biomolecular interaction analysis and its applications.
Why Study Biomolecular Interaction?
Interactions between biomolecules are a critical aspect of many biological processes. Whilst some proteins function on their own, most proteins are only active in complex forms. This means that their relationships with other biomolecules such as metals, lipids, proteins, and nucleic acids are extremely important.
Biomolecular interaction analysis looks at the physical contact between protein partners as well as the functional trends in signaling and metabolic pathways. Protein interactions and molecular interactions are intrinsic to all areas of cellular process such as:
- Regulation of metabolic pathways
- Cellular motion
- Signal transduction
- Environment sensing
With so many critical processes being informed by biomolecular interaction, the right form of analysis must be chosen.
Surface Plasmon Resonance SPR
SPR is a label-free method of biomolecular interaction analysis that works by using incident light to stimulate oscillating conduction electrons between positive and negative permittivity material. SPR measures adsorption onto planar metal or onto the surface of metal nanoparticles.
SPR is well-suited to measuring the affinity and selectivity of biomolecular interactions. It can be used for investigating association and dissociation rate constants and presenting the kinetics of biomolecular interactions. This technique can also be used for equilibrium binding analysis.
SPR does not require additional reagents, sample preparation, or assays and has high precision for classifying protein-protein interactions.[1]
Isothermal Titration Calorimetry
ITC is a method used for the quantitative study of a range of biomolecular interactions. This technique works by measuring the heat directly that is absorbed or released in a biomolecular binding event.
The main benefit of ITC is that it can determine each binding parameter concurrently in just one experiment and no modification of binding partners is required.
Bio Layer Interferometry BLI
BLI (biolayer interferometry) is an optical biosensing technology used for biomolecular interaction analysis. One of the key benefits of BLI is that it offers real-time label-free measurements for data analysis.
BLI studies macromolecular interactions, focusing on the interference patterns from white light reflected from the surface of the biosensor tip. It is a simple technique that measures Kon, Koff, and KD in just one rapid assay.
BLI is robust and easy to set up, it can be used for a range of samples including both crude and purified samples. This means that it can be used for a variety of investigations without needing to swap between systems for samples. Its small footprint means that it does not take up valuable space in the lab, making it more versatile than many other technologies.
BLI also allows for a broad variety of affinity values with the ability to investigate the following:
- Nanobodies
- Antibodies
- AAV
- Small molecules
- Nucleic acid
- Membrane proteins
Biomolecular Interaction Analysis from Gator Bio
Gator Bio stocks a range of BLI models suitable for biomolecular interaction analysis. It is a highly flexible, accessible, and sensitive technology that can characterize large varieties of proteins and molecules. If you would like to find out more about how our products could help with your biomolecular interaction analysis, read our dedicated page here.
[1] https://pubmed.ncbi.nlm.nih.gov/23533209/