Contract · No Set aside used
TECHNOLOGY LICENSING OPPORTUNITY: Bacterial Lipid Nanodiscs Platform
- Agency
- ENERGY, DEPARTMENT OF / ENERGY, DEPARTMENT OF
- Location
- Los Alamos, NM
- Amount
- Amount not listed
- Deadline
- Closes in 150 days (Dec 15, 2026)
- Posted
- Jun 15, 2026
- Set-aside
- No Set aside used
- NAICS code
- 541715
What this contract is for
The Bacterial Lipid Nanodiscs Platform developed by Los Alamos National Laboratory provides a new way to study entire bacterial membranes in a controlled, nanoscale format derived directly from native lipid extracts. Researchers gain access to membrane components that typically remain difficult to isolate, stabilize or analyze, enabling more accurate evaluation of immunogenic lipids and membrane?associated targets. The platform offers a safer alternative to handling live high?risk pathogens while preserving the biological context that drives meaningful insights for vaccine design and antimicrobial discovery such as therapeutic antibodies to conserved lipids on bacterial membranes. How it Works The Bacterial Lipid Nanodiscs Platform creates uniform nanoscale discs from total lipid extracts harvested from bacterial membranes. Membrane scaffold protein MSP1D1 encases the lipid mixture and forms a stable disc roughly 10 nanometers wide. The resulting particles retain the full complement of native bacterial lipids, arranged in a membrane?like environment that supports realistic biological interactions without requiring synthetic lipids or live cells. Technical Description The method adapts established nanodisc assembly techniques to incorporate entire bacterial lipid extracts rather than defined synthetic lipid mixtures. Total lipids from a pathogen are solubilized, combined with MSP1D1 and dialyzed under controlled conditions to allow the scaffold protein to form a discoidal structure around the heterogeneous lipid population. The process yields nanoparticles that represent the membrane environment of the source organism, including amphiphilic molecules that typically resist purification or structural study when isolated from their native context. The approach was demonstra...
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