Full-length membrane protein SPR services

The full-length membrane protein Surface Plasmon Resonance (SPR) is a biophysical analysis technique used to study the interactions between full-length membrane proteins and their ligands, such as small molecules, proteins, peptides, antibodies, and others. Investigating the interactions between full-length membrane proteins and their ligands is of great significance for drug development and biological research.

Surface Plasmon Resonance (SPR) is a method that quantitatively measures the changes in the resonance angle of polarized light (SPR Angle) at the liquid-solid interface when molecular complexes are formed, allowing for real-time detection of target molecules in a sample. Full-length membrane proteins, due to their strong hydrophobicity, often need to be embedded in phospholipid bilayers to maintain their native structure and function.

With years of experience in developing full-length membrane proteins, DIMA offers a wide range of products covering various families such as GPCRs, CLDNs, and ion channels. They provide over 1000 types of full-length membrane protein nanodiscs, all of which have been validated for activity and function. Based on the characteristics of full-length membrane protein nanodiscs, DIMA has developed specialized chips for immobilizing full-length membrane proteins, providing strong support for SPR detection in pharmaceutical companies and research institutions.

When a ligand binds to a full-length membrane protein, it induces a change in the refractive index on the chip surface. The SPR detector can monitor this change in real time, generating a sensorgram that is used to analyze the binding kinetics, such as the dissociation constant (KD), association rate constant (kon), and dissociation rate constant (koff).

The key challenges in SPR detection of full-length membrane proteins lie in determining the immobilization and detection methods. Traditional chips often struggle to effectively immobilize full-length membrane proteins while maintaining their orientation and functionality. To address this issue, Dima Biotechnology, leveraging its deep understanding of full-length membrane protein characteristics, has developed various methods to support SPR detection of full-length membrane proteins. Dima has invested significant effort in establishing an SPR detection method suitable for full-length membrane protein nanodiscs, launching an SPR analysis and testing service for full-length membrane proteins. This service provides customers with a mature and reliable solution, helping them avoid difficulties in finding appropriate SPR methods due to unfamiliarity with full-length membrane protein nanodisc characteristics. Additionally, some clients who have outsourced SPR services to traditional CRO companies often encounter repeated failures due to a lack of deep understanding of full-length membrane protein nanodiscs. We welcome researchers to inquire for further details.

• 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.

• 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.

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

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

How to Participate:

Click the button to download the Molecular Interaction Service Request Form. After completing the form, please send it to the email: info@dimabio.com. Dima Bio staff will contact you within 24 hours.