Recombinant Human MSP protein

Membrane Scaffold Protein (MSP) recombinant proteins are engineered polypeptides central to the formation of nanodiscs, a groundbreaking tool in membrane protein research. Derived from apolipoproteins, particularly human apolipoprotein A-I, MSPs are amphipathic alpha-helical molecules that self-assemble with lipids to create stable, soluble discoidal lipid bilayers. These nanodiscs mimic native cell membrane environments, enabling the isolation and study of membrane proteins—such as receptors, transporters, and enzymes—in a functional, water-soluble state.

The development of MSPs, pioneered by Stephen G. Sligar’s group in the early 2000s, addressed longstanding challenges in handling membrane proteins, which are notoriously difficult to stabilize outside lipid bilayers. Recombinant DNA technology allows customizable MSP production, with variants like MSP1D1 and MSP1E3D1 offering tunable nanodisc sizes (5–17 nm) by altering the number of helical repeats. This flexibility accommodates diverse membrane proteins and complexes.

MSP-based nanodiscs have revolutionized structural biology (e.g., cryo-EM and X-ray crystallography), drug discovery, and functional studies by preserving protein conformation and activity. They also facilitate high-throughput screening of membrane protein-targeted therapeutics and enable investigations into lipid-protein interactions. Recent advances include hybrid nanodisc systems and conjugation strategies for biotechnological applications like biosensors or targeted drug delivery.

Despite their utility, challenges persist in optimizing homogeneity and scalability. Ongoing research focuses on expanding MSP versatility, such as pH-responsive designs or modified lipid compositions, to better replicate complex cellular membranes. MSP technology continues to bridge the gap between in vitro and in vivo studies, underpinning innovations across biochemistry and medicine.