Description:
Membrane proteins (MP) mediate many of the cell’s fundamental processes and MPs are embedded in the cell’s membrane lipid bilayer. Currently, MPs are targets for about 60% of therapeutic drugs in use.
However, MPs are very difficult to manipulate and study because they require both an aqueous environment and need transmembrane hydrophobic regions. Because this is tricky and difficult to achieve, most studies use the protein solubilized in detergent. Because of this particular setup, these study systems have limited stability.
To address this, the industry has used liposomes (i.e., the lipid bilayer) as traditional platforms for MP. Further, the industry has capitalized on the use of nanodiscs. Specifically, engineering a derivative of apolipoprotein A-1 as a membrane scaffold protein (MSP). Although liposomes and nanodiscs are MP-supporting platforms, their broad utility is limited by the fluidic and labile nature of the lipid bilayer in these set-ups.
This technology provides two new platforms for MPs. Overall, the new platforms will have controlled compositions and properties that can support MPs without compromising the structure and function of MPs. Hence, applications may include, but are not limited to, functional and structural studies of MPs, biotechnology, biomedicine, pharmaceutical, targeted therapy, and industrial enzymatic processes.
Reference Number: D-1303
Market Applications:
•Biotechnology
•Biomedicine
•Pharmaceutical: Drug discovery, targeted therapy
•Industrial enzymatic processes
Features, Benefits, & Advantages:
•Replaces the fluidic/labile nature or existing lipid bilayers of liposomes and nanodiscs
•Broad utility
•Flexibility
•Provides a research platform that gives stability to membrane proteins
Intellectual Property: A US provisional patent, serial number 62559706, was filed on 9/18/17.
Development Stage: The invention has been reduced to practice.
Researchers:
•Guillermo Altenberg, Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center School of Medicine, Lubbock, Texas
•Hongjun Liang, Cell Physiology and Molecular Biophysics, Texas Tech University, Lubbock, Texas
Keywords: Membrane proteins, drug discovery, stability