Detergent-Free Nanodiscs for Better Drug Discovery

An SMA nanodisc is a uniform soluble nanoparticle where a multi-pass transmembrane protein is encapsulated by a Styrene-Maleic Anhydride (SMA) synthetic polymer. This synthetic polymer is added directly to the cell membrane, where it cuts out and wraps a patch of native membrane, protein and all. This gentle process avoids extraction interferences and keeps the target protein in its endogenous lipid environment.

Detergents can strip away annular lipids and often push proteins into non-native conformations. Traditional MSP (membrane scaffold protein) nanodiscs also require the target protein to first be purified in detergent, subjecting it to a fragile detergent window before it is rebuilt into artificial lipids. Our SMA platform bypasses detergents entirely, keeping the protein's native lipids and true native conformation intact. This detergent-free approach retains protein activity for days to weeks, whereas detergent micelles degrade over minutes to hours.

We express our recombinant multi-pass membrane proteins in HEK293 cells. We utilize mammalian cells because they more faithfully replicate native protein folding and provide crucial post-translational modifications (such as glycosylation) that are necessary for complex multi-pass targets.

Yes, His-tags and biotinylation tags are available on our nanodisc proteins to seamlessly integrate into your specific capture workflows.

Our nanodiscs provide consistent lot-to-lot performance and biological relevance essential for therapeutic antibody drug discovery and development. They are utilized for antibody screening and functional characterization at the molecular level. The platform is validated for standard assays including SPR, BLI, and ELISA. Because the protein reaches the sensor surface in its native lipid environment, binding kinetics reflect true affinity rather than an artifact of reconstitution.

Yes. We offer custom production for full-length, multi-pass membrane proteins. We express your custom target in mammalian cells to ensure proper folding and correct post-translational modifications. We then utilize our detergent-free SMA platform to extract and encapsulate the protein, delivering your target securely locked in its native conformation.

Our platform is highly tailored for complex multi-pass transmembrane proteins (proteins with two or more transmembrane helices). While researchers can often get away with using just the extracellular domain (ECD) for single-pass proteins, multi-pass targets generally need to be studied full-length. Because these complex proteins aggregate readily outside of a membrane and depend heavily on their surrounding lipid environment for their 3D conformation, our native nanodisc environment is essential for their stability and functional characterization.

Absolutely. AI-generated binders are typically designed against a modeled or predicted epitope. If you screen these against a target that has been distorted by detergents or artificial lipid reconstitution, you risk generating false negatives (real binders that fail) or false positives (binders that only recognize an artifact of reconstitution). Because our SMA copolymer nanodiscs preserve the true native state and endogenous annular lipids, they provide the strict conformational fidelity required for accurate binding-affinity work.

Because SMA copolymers extract whatever patch of native membrane they happen to wrap, they are less uniform in size and defined composition than MSP discs. While this modest particle heterogeneity is highly tolerated by applications like ELISA or SPR, copolymer discs are not ideal for applications requiring tight particle-to-particle consistency, such as high-purity Cryo-EM alignments.