The activity of biologics such as proteins, monoclonal antibodies, recombinant proteins, therapeutic peptides, etc., is often based on molecular interactions with specific receptors or target molecules in the human body. Robust characterization of the binding properties of these biopharmaceuticals to target antigens is critical to ensure therapeutic success. With surface plasmon resonance (SPR) technology, CD Formulation can help you identify the best therapeutic candidates and reliably and in detail characterize the specificity and strength of the interaction of drug products with targets to ensure that your biologics are fully characterized as well as meet regulatory guidelines, no matter where you are in the project life cycle.
SPR is a powerful optical detection technique that can be used to study the binding behavior of immobilized ligands and analytes in solution. This technique can quantitatively measure binding events in real-time without labeling the interacting molecules and has become the gold standard for studying biomolecular interactions in biomedical research and drug discovery. As an innovative tool for studying biomolecular interactions, such as protein-protein, protein-small molecule, protein-nucleic acid, protein-carbohydrate, lipid-protein, etc., SPR plays a vital role in the discovery and development of protein and peptide biotherapeutics and is suitable for early candidate drug screening and preclinical bioactivity assessment. The advantage of SPR is that it only requires a minimal amount of sample, does not require sample pretreatment, and has high throughput and high sensitivity.
The principle of SPR is an optical measurement concept of total internal reflection. In SPR, light passes through a prism and is reflected from the surface of the sensor chip into the detector at a specific angle of incidence (called the resonance angle). The light is absorbed by the electrons on the surface of the sensor chip. There are certain changes in the SPR reflection intensity curve, such as the shape and position of the curve drop, which can provide information about the surface. The binding of biomolecules causes a change in the refractive index on the sensor chip, which is proportional to the concentration of the bound analyte on the surface of the biosensor chip, thereby plotting the relationship between the response and time and generating a sensor map.
A critical step in SPR analysis is the immobilization of the ligand to the surface of the biosensor chip. Immobilization of the ligand can be achieved by direct covalent coupling to the chip surface or by capture with the aid of pre-coated capture molecules. However, direct covalent immobilization of the ligand can alter its biological activity or result in non-directional immobilization, which reduces the accessibility of the binding sites. Transient immobilization of the labeled ligand by affinity capture molecules overcomes these drawbacks.
Fig. 1 The concept of surface plasmon resonance. (Motsa B B, et al., 2023)
Thanks to decades of experience leveraging SPR to support protein/peptide biotherapeutic development, CD Formulation is able to collaborate on your early-stage and downstream strategies to ensure your biotherapeutic products successfully enter the clinical stage and market.
Our team can help you optimize applications for many different projects to ensure consistent results with the shortest turnaround time, and our dedicated scientific experts provide access and insights into state-of-the-art technologies.
Our analytical laboratories are equipped with world-class SPR instrumentation, providing rapid, sensitive and reliable assays for applications such as affinity measurements, pharmacokinetics (PK), toxicokinetics (TK), immunogenicity, biopotency testing (batch release and stability testing), drug screening, and more.
Utilizing cutting-edge SPR technology, we can help you make informed decisions during the following stages of protein and peptide drug discovery and development:
The key to identifying the best therapeutic candidate drug includes determining the binding kinetics and affinity of the biologic. We can perform preliminary affinity ranking of candidate proteins/peptides in culture or purified, and make preliminary judgments on the specificity and kinetic characteristics of proteins/peptides, thus accelerating the screening of candidate drugs.
Protein-based biological drugs are immunogenic, and repeated administration can cause the body to produce anti-drug antibodies. Anti-drug antibodies may form complexes with drugs, neutralize their activity or affect their normal metabolism. Our scientists use SPR technology to accurately detect the immunogenicity of antibodies even at low concentrations.
Activity assay is an important indicator for evaluating the efficacy of active ingredients in protein/peptide drugs, mainly evaluating the ability of drugs to bind to target receptors. In addition to ELISA assays, we also provide SPR technology to further understand the affinity and kinetic characteristics of protein and peptide drugs, as well as to preliminarily determine the metabolism of drugs in the body.
We use SPR technology to evaluate the batch-to-batch consistency of drugs to ensure that the quality of drugs can be controlled during the production process.
Real-time monitoring of bioreactors using online measurements is a viable option for SPR technology because the lengthy preparation and analysis times required by alternative techniques (ELISA, Western blot, bioassays) are not required. Our scientists use SPR technology to monitor the concentration and bioactivity levels of protein and peptide drugs in real-time during upstream and downstream processing.
Published Data
Technology: SPR
Journal: Sci Rep.
IF: 3.8
Published: 2019
Results:
The authors developed a novel SPR-based technology for therapeutic drug and immunogenicity monitoring (TDIM), which is used to measure the concentrations of IFX and ATI in serum. The sensitivity and reproducibility of the SPR assay were evaluated and applied to measure the TL of IFX and ATI in 15 patients treated for inflammatory bowel disease (IBD). The SPR results were compared with those generated by commercial ELISA kits. The results showed that the novel SPR has a clear advantage, which can directly detect and measure serum antibodies within minutes, reducing complexity and variability. In addition, drug and anti-drug antibodies can be measured simultaneously.
Fig. 2 General scheme of the SPR-based assay for simultaneous determination of IFX and ATI concentrations in serum. (Beeg M, et al., 2019)
CD Formulation aims to provide a powerful analytical tool for characterizing biomolecular interactions, assessing binding affinities, and studying kinetics of ligand-receptor interactions. Please feel free to contact us if you are interested in our services. Learn how our SPR technology can support the smooth implementation of your protein/peptide biopharmaceutical program.
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