The Nanodisc system has proven to be a widely applicable means for rendering membrane proteins soluble in aqueous solution and, importantly, in a native-like bilayer environment where they remain monodisperse and active. Some appreciation for the diversity of membrane proteins systems that can be self-assembled into Nanodiscs is evidenced from the Rogue's Gallery below:
We have published several review articles over the past five years that summarize these successes and provide the protocols for use of Nanodiscs. Some of these are available through the PubMed links below:
We remain committed to the widest possible dissemination of the Nanodisc technology, including materials, methods and latest data from our laboratory. The Nanodisc system is now being used by dozens of laboratories around the world that have realized great success and further advanced the technology.
In order to provide a common reference point for the various MSPs that have been utilized to self-assemble proteins, we provide the following link:
The critical component of Nanodiscs is the encircling amphipathic helical protein belt. Although almost any amphipathic polypeptide will assemble lipids into lipoprotein particles, our extensive work over the past decade has shown the importance of sequence and lipid stoichiometry in generating homogeneous and monodisperse entities. In order to provide our membrane scaffold proteins to as large an audience as possible, out synthetic genes for expressing large quantities of membrane scaffold proteins (MSPs) in E. coli are easily available from AddGene (just search Sligar):
To date there have been over three hundred requests for these genes from members of the academic community. A detailed procedure for growth and expression of MSPs is available either through the publications sited above or the link below:
We are also happy to provide small quantities (~50 mg) of purified membrane scaffold proteins for all academic researchers to try out this technology, as long as supplies are available. However, according to University policy this necessitates a time consuming administrative paperwork of a Materials Transfer Agreement. This is administered by the Office of Technology Management on the UIUC campus with the contact information provided below.
An overview of the Nanodisc methods and guidance for self-assembling your favorite target protein into lipoprotein particles can be obtained through the following link:
You can now buy reagants and materials you may need to assemble membrane proteins into Nanodiscs from Sigma-Aldrich.
Nanodisc technology, and many of its uses, are covered by a broad intellectual property portfolio. Currently, the following patents have issued:
|7,691,414||Membrane scaffold proteins|
|7,662,410||Membrane scaffold proteins and embedded membrane proteins|
|7,622,437||Tissue factor compositions and methods|
|7,592,008||Membrane scaffold proteins|
|7,575,763||Membrane scaffold proteins and tethered membrane proteins|
|7,083,958||Membrane scaffold proteins|
|7,048,949||Membrane scaffold proteins|
The licensing rights to the entire intellectual property suite related to Nanodisc technology is held by the University of Illinois, and not by any private entity. At present, no exclusive licenses have been granted to the private sector, although some non-exclusive licenses are in place. The University’s Office of Technology Management is actively seeking the licensing and commercialization of this technology. Information for licensing Nanodisc technology for commercial, or for Materials Transfer Agreements, please contact:
Office of Technology Management
University of Illinois Urbana-Champaign
319, Ceramics Building MC-243
105 S. Goodwin Avenue
Urbana, IL 61801-2901
Phone: (217) 333 7862
Fax: (217) 265 5530
If you need any further assistance, please do not hesitate to contact Dr. Sligar, our senior technical person for MSP production and Nanodisc assembly (Yelena Grinkova: email@example.com) or our laboratory manager (Aretta Weber: firstname.lastname@example.org).