In this webinar, the featured speakers will introduce the application of synthetic co-polymer nanodisc to solubilize and stabilize membrane proteins for further characterization.
Integral membrane proteins are essential for cellular function. Sitting at the edge of the cell, they are the first point of contact between cells and their environment. As such, they mediate how cells sense and interact with their surroundings, communicate with other cells and tightly control what gets in or out. Not surprisingly, they are also the linchpin of the pharmaceutical industry.
Although they represent about a third of the proteins encoded in the human genome, they are targeted by roughly 70% of the currently approved drugs. Unfortunately, at par with their biomedical relevance is the difficulty of characterizing them. To do so has traditionally involved removing them from their native environment and replacing the membrane with detergents. Alas, detergents are a poor replacement for the membrane, often leading to loss of stability and function. Moreover, finding the best detergent is a time-consuming process. Even with access to the best detergent, excess detergent is a necessity, which can affect downstream applications.
Polymers — made of alternating acidic and hydrophobic groups — can integrate into the membrane and self-assemble so-called native nanodisc. All of this happens in a single-step reaction, without ever using detergents. By keeping the membrane protein always surrounded by their native lipids, function should be preserved.
In the webinar, the featured speakers will discuss these results, including the main differences between classes of polymers, and show how some of them can rival classical detergents in performance and versatility. Using selected examples, they will also show how reconstituting proteins into native nanodiscs is compatible with many downstream applications, including the characterization of protein-ligand binding and structural determination through cryo-electron microscopy (cryo-EM).
Finally, they will discuss Cube Biotech’s GentleLys buffers. Leveraging the power of co-polymers, these buffers can quickly lyse eukaryotic cells and even directly stabilize membrane proteins. By avoiding mechanical or harsh chemical lysis strategies, fragile interactions of cellular components are better preserved, minimizing the risk of interference with subsequent analyses and improving compatibility with downstream assays.
Join this webinar to gain insights into the application of synthetic co-polymer nanodisc to solubilize and stabilize membrane proteins for further characterization.
Dr. Mario Leutert, Postdoctoral Researcher, Institute of Molecular Systems Biology at ETH Zurich
Dr. Mario Leutert is a Postdoctoral Researcher at the Institute of Molecular Systems Biology at ETH Zurich. He completed a postdoctoral fellowship at the University of Washington’s Department of Genome Sciences, received a PhD in Molecular Life Sciences from the University of Zurich, and a master’s degree in biotechnology from ETH Zurich.
His research centers on the development of technologies that permit proteome-wide characterization of cellular signaling and protein regulatory networks, including biochemical techniques, mass spectrometry methods and computational approaches. Using these strategies, he intends to comprehend the wiring diagram of the cell, thereby identifying and reversing changes that occur during aging and disease.
Dr. Felipe Merino, Head of Cryo-EM, Cube Biotech
Dr. Felipe Merino is the head of Cube Biotech’s Cryo-EM division, where he oversees several of their structural biology services. With a long track record in structural biology and biochemistry research, he also is a key part of Cube’s research and development team.
Dr. Merino obtained his PhD at the Max Planck Institute for Molecular Biomedicine Münster working on macromolecular modelling and simulation. He later became an expert in electron cryomicroscopy through his postdoctoral training at the Max Planck Institute for Molecular Physiology in Dortmund and as a project leader at the Max Planck Institute for Biology in Tübingen. His combined expertise in atomic modeling and cryo-EM has provided him with a unique skill set allowing him to tackle challenging structural biology problems, such as those typically presented by membrane proteins.
Who Should Attend?
This webinar will appeal to professionals from pharmaceutical and biotechnology companies, and academia interested in:
- Membrane protein purification
- Membrane protein structure characterization
- Proteomics and mass spec
- Drug development for membrane protein targets
What You Will Learn
During this webinar, attendees will learn:
- The key bottleneck of membrane protein research is finding solubilization and stabilization conditions that preserve the native structure and function of the protein
- Synthetic co-polymers — such as styrene-maleic anhydride (SMA), di-isobutylene maleic acid (DIBMA), acrylic acid-co-styrene (AASTY) and UltrasoluteTM Amphipols — can extract membrane proteins and their surrounding lipids directly from the membrane, self-assembling into a so-called native nanodisc
- State-of-the-art copolymers have solubilization efficiencies that rival those of detergents, while simultaneously providing superior stabilization and preserving native function
- The power of synthetic polymers can be leveraged to lyse eukaryotic cells
Unleashing the power of proteins for research and progress, Cube Biotech supports the pharmaceutical and biotechnical community with all its scientific expertise. By leveraging the latest technologies and techniques, we provide a comprehensive range of products and services that address the full spectrum of protein research, from expression and purification to characterization and stabilization.