Surface Plasmon Resonance (SPR) Service

Background

What is Surface Plasmon Resonance (SPR)?

Surface plasmon resonance (SPR) is an optical method used to figure out what things are made of and how they are structured. It works by checking out how a ligand and an analyte interact on biosensor chips. Basically, SPR happens when light hits a metal surface and creates some sneaky evanescent waves. When the frequency and wave number of evanescent waves are equal to that of surface plasma waves generated by free electrons on the metal surface, the two will resonate, resulting in the absorption of incident light, a sharp decline in reflected light energy, and a formant peak on the reflection spectrum. The position of this formant is related to the refractive index of the medium immediately adjacent to the surface of the metal film, so when the biomolecules bind to the film on the surface of the metal or interact with the adsorbed molecules, the characteristics of this plasma wave will change, resulting in a shift in the resonance Angle, so that the process of biomolecular interaction can be monitored.

Fig. 1. Schematic of the surface plasmon resonance (SPR) phenomenon and SPR biosensor experimental rationale. (Xie, et al., 2024)

Advantages of SPR

SPR technology offers a number of significant benefits, including:

• Real-time detection: SPR technology can dynamically monitor the whole process of biomolecular interaction and provide real-time data.
• Labeling free monitoring: The molecular activity is maintained, and the sample needs very little, generally only 100 μg protein on a surface.
• The detection process is convenient and fast: high sensitivity, wide range of applications, and high-quality analytical data.
• High sensitivity and specificity: SPR technology can detect extremely low concentrations of biomolecules, providing precise data and reliable results.
• Wide application range: SPR technology has wide application and important value in drug discovery, drug screening, protein-protein interaction research, antibody-antigen binding and other fields.

What is SPR Used for?

SPR technology plays a key role in the study of biomolecular interactions by enabling:

• Optimize the preparation technology of nanoparticles: In the preparation process of nanoparticles, SPR technology can monitor the synthesis reaction and surface modification in real time, and optimize the preparation technology and conditions.
• Precise measurement of intermolecular interactions: including binding affinity and kinetic parameters to evaluate the properties of nanoparticles.
• Widespread use in biomedical applications: SPR technology is widely used in drug delivery systems, biomarker detection for disease diagnosis, and research on nanoparticle-biomolecular interactions.
• High spatial resolution SPR Imaging technique: Researchers have successfully used this high spatial resolution SPR imaging technique to image and detect individual DNA molecules, viruses, cells, as well as maps of single-cell-matrix interactions and direct protein-cell membrane protein binding dynamics.

Service Procedure

Platforms

SPR technology, being the top method for spotting how biomolecules interact, needs some pretty sophisticated gear and scientific know-how. At Creative BioMart, we’ve got a wide array of SPR devices to handle detection across different materials and conditions. Add in our thorough analysis skills—checking how things stick together, measuring kinetic parameters, evaluating specificity and selectivity, and running temperature and thermodynamic checks—and we can offer our clients deep insights and top-notch data for every step, from the basics to developing new drugs.

Service Contents

Drug Discovery and Screening Services

In the realm of drug discovery and screening, we offer an all-encompassing suite of services. Our offerings include small molecule-target interaction analysis for deeper insights into drug mechanisms and lead optimization, as well as antibody screening and refinement, utilizing high-throughput SPR technology for qualitative and quantitative analyses of antibodies and Fab fragments to accelerate biopharmaceutical development. We conduct comprehensive affinity and kinetic analyses of biologics, thoroughly exploring the binding characteristics of molecules. Additionally, we provide drug-protein binding kinetics studies, accurately determining affinity and kinetic rate constants essential for drug development pipelines. Our services span the entire process—from target discovery to lead drug selection and optimization—leveraging advanced SPR technology to furnish clients with efficient and precise drug discovery and screening solutions.

Biomarker Study Services

In biomarker research, we’re all about using SPR tech to spot disease-linked molecules and nail down new biomarkers. This lets us check out how biomolecules interact in real time, even in complicated samples without preprocessing. That means the results are super reliable. We can spot all sorts of interactions like protein pairing with proteins, nucleic acids, drugs, and receptors, which helps in drug discovery, understanding protein roles, making antibodies, and advancing biosensors. Our work in this area helps sift through new biomarkers, paving the way for early disease diagnosis and treatment. Plus, we can check how antibodies connect with receptors, which is key to understanding the bioactivity in developing antibody drugs.

Biosensor Development Services

In biosensor development, our SPR services are all about boosting sensitivity and specificity. With SPR’s high sensitivity, we can pick up on tiny changes in refractive index within biological samples, making biosensors more responsive. We also track how reflected light intensity changes over time to dive into interactions like protein-protein, protein-nucleic acid, and protein-small molecules. This helps us understand how biosensors function. Plus, we analyze binding specifics like whether it happens, how selective or strong it is, the speed of binding and unbinding, stability, temperature effects, and overall molecular activity.

Materials Science Research Services

In materials science, using SPR technology to understand how molecules behave at surfaces is a big deal. We dig into how nanomaterials and proteins link up at the molecular level, helping researchers grasp their structural and property changes. Plus, our research explores how big biomolecules mix with material surfaces. This lays the groundwork for creating materials with specific biological functions and refining techniques for protein separation, purification, and biodetection.

Our Advantages

• Advanced technology platform. Use a variety of high-end SPR devices, such as the Biacore family, to support complex molecular interaction studies and high-throughput screening.
• High quality data assurance. Provides accurate kinetic, affinity and thermodynamic analysis with specialized analysis software and detailed reports.
• Flexible customization services. It has comprehensive solutions from experimental design to sample handling and data analysis to meet diverse needs.
• Professional team and efficient delivery. The experienced team ensures rapid experimental delivery and provides ongoing technical support and training services.

Case Study

Background

The Service is for SPR binding assay to measure binding affinity K _D of protein interaction with small compound. The ligand is protein which need to be printed onto the chip. The analyte is small compound. All samples were provided by Customer while reagents and consumables were provided by Creative BioMart.

Methods

The ligand was immobilized on Sensor chip CM5. The protein was injected at a flow rate of 5 μL/min. Wash the Biacore system pipeline with PBS-P buffer (PBS with 0.05% (v/v) surfactant P20). Various concentrations of analytes were loaded into Biacore 3000 injector and set the setting parameters as follows: contact time=120 s; dissociation contact time=30 s; flow rate=30 μL/min. Run the program to determine the binding affinity between analytes and ligands. Data analysis was performed using BIAevaluation software.

Results

Evaluation of the binding affinity of protein to compound according to the steady-state analysis fitting curve. The equilibrium dissociation constant (K _D Value) was 3.92×10 ^-5 M.

Fig. 2. SPR result of protein to small compound.

FAQs

• Q: Is SPR technology suitable for affinity detection of small molecule compounds?

  A: Yes, SPR technology is suitable for affinity detection of small molecule compounds, but it is necessary to judge whether solvents such as DMSO are needed according to the solubility of small molecules.

• Q: What are the precautions of SPR technology in affinity detection?

  • Disinfection of the instrument is required after testing of the virus sample to prevent possible damage to the instrument caused by microorganisms in the pipe.
  • The buffers commonly used for affinity analysis are PBS or HBS, and there are special requirements for protein buffers, such as not containing EDTA or Tris.
  • Small molecule compounds can be tested for affinity, but may require dissolution with DMSO and solvent correction.
  • The problem of non-specific binding can be solved by centrifugation, cleaning, filtration and cell density adjustment.

References:

• Xie J.; et al.  Advances in surface plasmon resonance for analyzing active components in traditional Chinese medicine. J Pharm Anal.  2024;14(10):100983.
• Samadi Pakchin P.; et al . Recent advances in receptor-based optical biosensors for the detection of multiplex biomarkers. Talanta . 2025;281:126852.