Surface Plasmon Resonance (SPR) Service for Membrane Proteins

Surface Plasmon Resonance (SPR) is a powerful biophysical technique used to study molecular interactions in real time. It is particularly valuable for investigating interactions between membrane proteins and their ligands, such as small molecules, peptides, antibodies, proteins, and others. SPR provides crucial insights into binding kinetics, affinity, and specific interactions, making it an essential tool for drug discovery, biomarker identification, and biological research.

DIMA’s Nanodisc-Based SPR Service Highlights:

  • 1,000+ nanodisc proteins available as standard catalog items
  • Specialized SPR service tailored to nanodisc-proteins
  • Ideal for multi-pass transmembrane proteins like GPCRs and ion channels etc. 

How SPR Service Works?

Surface Plasmon Resonance (SPR) is a label-free technique that measures real-time changes in the refractive index at the liquid-solid interface when molecular interactions take place. By monitoring the resonance angle of polarized light, SPR provides quantitative insights into biomolecular binding, enabling real-time detection of target molecules in a sample.

Full-length membrane proteins are inherently hydrophobic, requiring embedding in phospholipid bilayers (e.g., nanodiscs) to preserve their native structure and function. DIMA Biotechnology offers 1,000+ validated full-length membrane protein nanodiscs, covering a broad range of protein families, including GPCRs, ion channels, and CLDNs. 

Using specialized SPR chips developed by DIMA, nanodisc proteins are immobilized for precise and high-quality interaction analysis. When a ligand binds to a protein, it induces a change in the refractive index at the sensor surface, which is monitored in real time. This generates a sensorgram for detailed analysis of binding kinetics, including the dissociation constant (KD), association rate constant (kon), and dissociation rate constant (koff). This data provides valuable insights into the strength, specificity, and dynamics of ligand-protein interactions, supporting drug discovery and biologics development.

SPR Technology Detection Principle

GPCR Proteins

CLDNs Protein

Ion Channel Proteins

Applications

Challenges & Solutions

One of the key challenges in SPR detection of full-length membrane proteins is effectively immobilizing them while preserving their native structure and functionality. Traditional SPR chips often struggle to maintain proper orientation and activity of membrane proteins during immobilization.

DIMA’s Solution
To address these challenges, DIMA Biotechnology has leveraged its expertise in membrane protein science to develop specialized methods for SPR analysis. We have invested significant resources into creating optimized SPR protocols for full-length membrane protein nanodiscs, offering a reliable, turnkey service for SPR analysis. This service provides customers with a proven solution, enabling them to bypass the difficulties of adapting traditional SPR methods for membrane proteins.

Many researchers who outsource SPR analysis to conventional CROs often face repeated failures due to a lack of understanding of membrane protein nanodiscs. At DIMA, we offer a deeper level of expertise and support, ensuring successful results. We encourage researchers to reach out for more information or to inquire about our services.

Successful Cases

  • Case 1: Affinity Measurement of Full-Length Membrane Protein with Therapeutic Antibody

When screening therapeutic antibodies targeting multi-pass full-length membrane proteins, it is essential to select antibodies with high affinity to ensure better functional properties. By measuring and comparing the SPR activity between antibodies and full-length membrane proteins, an effective solution can be provided for selecting high-quality therapeutic antibodies.

Magrolimab（SKU: BME100001 ) binding with Human CD47 (SKU: FLP100039) with an affinity constant of 0.168 nM

  • Case 2: Affinity Measurement of Full-Length Membrane Protein and Peptide

The activity testing of full-length membrane proteins expressed in synthetic nanodiscs binding to peptides is also a common method for detecting biomolecular interactions.

Peptide binding with Synthetic Nanodisc with an affinity constant of 40.8 nM

  • Case 3: Affinity Measurement of Full-Length Membrane Protein and Peptide

Activity testing of the binding between therapeutic antibodies and full-length membrane proteins.

IMAB-362 (BME100075) bind with Human CLDN18.2-Nanodisc an affinity constant of 1.619 nm.

Service Process

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If you have available evidence for estimating the interaction force or reference literature, please provide it.

Sample Preparation Guidelines:

  • Purity: Samples should have >90% purity.
  • Concentration: Ligands and analytes should be >0.5 μg/μL, with at least 200 μg provided. For small molecules, please provide 1-5 mg.
  • Buffer & Solvent: Avoid reagents like Tris, metal ions, SDS, Triton X-100, glycerol, or DMSO unless absolutely necessary.
  • Samples should be free from particles or precipitates.
  • Protectants: Avoid protectants such as trehalose, BSA, or sucrose. If these are necessary, their final concentration should be ≤ 0.1% after dilution.
  • Lyophilized Samples: For lyophilized powder, confirm it can dissolve in 10 mM HEPES (pH 7.4) or provide the buffer used before lyophilization.
  • Samples must not contain radioactive, infectious, or hazardous components.
  • If the ligand’s buffer is incompatible with chip immobilization, we may need to replace it, which could incur additional charges.