| A -- TECHNOLOGY/BUSINESS OPPORTUNITY Cell-Free Assembly of NanoLipoprotein Particles |
| Program Summary |
 |
| Description |
|
General Information
| Document Type: |
Special Notice |
| Solicitation Number: |
Reference-Number-FBO165-08 |
| Posted Date: |
Feb 11, 2008 |
| Original Response Date: |
Mar 12, 2008 |
| Current Response Date: |
Mar 12, 2008 |
| Original Archive Date: |
Mar 13, 2008 |
| Current Archive Date: |
Mar 13, 2008 |
| Classification Code: |
A -- Research & Development |
| Naics Code: |
238990 -- All Other Specialty Trade Contractors |
Contracting Office Address
Department of Energy, Lawrence Livermore National Laboratory (DOE Contractor), Industrial Partnerships & Commercialization, 7000 East Avenue L-795, Livermore, CA, 94550, UNITED STATES
Description
TECHNOLOGY/BUSINESS OPPORTUNITY
Cell-Free Assembly of NanoLipoprotein Particles
Opportunity: Lawrence Livermore National Laboratory (LLNL), operated by the Lawrence Livermore National Security (LLNS), LLC under contract with the U.S. Department of Energy (DOE), is offering an opportunity to license a new method of cell-free self-assembly of nanolipoprotein particles (NLPs) as a platform for expressing functional membrane proteins along with a colorimetric assay based on bacteriorhodopsin (bR) that indicates direct incorporation of functional membrane protein.
Background: Membrane-associated proteins and protein complexes account for roughly one-third of the cellular proteins. These protein complexes mediate essential cellular processes such as signal transduction, transport, recognition, and cell-to-cell communication. This class of proteins is difficult to study because of their insolubility and tendency to aggregate when removed from their protein-phospholipid lipid bilayer environment. Also, over-expression of membrane proteins in vivo often results in cell toxicity, protein aggregation, mis-folding and low yield.
Description: LLNL has developed a novel process of production, isolation, characterization, and functional re-constitution of membrane-associated proteins in a single step. In addition, LLNL has developed a colorimetric assay that indicates production, correct folding, and incorporation of bR into a soluble nanolipoprotein particles (NLPs).
? LLNL has developed an approach, for formation of NLP/membrane protein complexes by simultaneous co-expression of both apolipoprotein and target membrane protein in a cell-free protein synthesis system. This approach involves cell-free transcription/translation technology adapted to co-express both apolipoproteins and a target membrane protein. It is carried out in a single reaction chamber with cell extract, buffer, phospholipds, detergents and the like to facilitate stabilization; the entire process can be complete in a few hours.
Advantages:
? Cell-free protein synthesis technology allows simultaneous expression of apolipoproteins and membrane proteins leading to self-assembly of nanolipoprotein particles containing soluble and functional proteins within a stable membrane mimetic. .
? Cell-free method of simultaneous co-expression of both apolipoprotein and target membrane can be achieved in a single step.
? Process can be completed in a few hours .
? Increase yields of stable, soluble and functional membrane proteins for downstream characterization.
? Membrane proteins are expressed rather than purified from cellular sources.
Commercial Uses:
? Rapid production of novel functional membrane proteins that are difficult to obtain from native systems
? Process screening of parameters for evaluation of production of membrane proteins
? Medical diagnostics, therapeutics, biofuels
Development Status: LLNL has used cell-free expression for single step production and refolding of the membrane protein bacteriorhodopsin. This unique approach has been demonstrated by the co-expression of a truncated apolipoprotein and the bacteriorhodopsin gene, which resulted in a functionally active seven trans-membrane helix spanning bacteriorhodopsin protein containg co-factor retinal. In addition, LLNL has developed a colorimetric assay that indicates production, correct folding and incorporation of bacteriorhodopsin into soluble nanolipoprotein particles.
LLNL has filed provisional patent applications on these technologies.
LLNL is seeking industry partners with a demonstrated ability to bring such inventions to the market. Moving critical technology beyond the Laboratory to the commercial world helps our licensees gain a competitive edge in the marketplace. All licensing activities are conducted under policies relating to the strict nondisclosure of company proprietary information.
Please visit the IPAC website at: https://ipo.llnl.gov/workwithus/partneringprocess.php
for more information on working with LLNL and the industrial partnering and technology transfer process.
Note: THIS IS NOT A PROCUREMENT. Companies interested in commercializing LLNL?s Cell-Free Assembly of Nanolipoproteins should provide a written statement of interest, which includes the following:
1. Company Name and address.
2. The name, address, and telephone number of a point of contact.
3. A description of corporate expertise and facilities relevant to commercializing this technology.
Written responses should be directed to:
Lawrence Livermore National Laboratory
Industrial Partnerships Office
P.O. Box 808, L-795
Livermore, CA 94551-0808
Attention: FBO 165-08
Please provide your written statement within thirty (30) days from the date this announcement is published to ensure consideration of your interest in LLNL?s Cell-Free Assembly of Nanolipoproteins
Point of Contact
Connie Pitcock, Administration, Phone 925-422-1072, Fax 925-423-8988, Email pitcock1@llnl.gov
|
|
