SPECIAL NOTICE
A -- TECHNOLOGY/BUSINESS OPPORTUNITY Improved Expression and Purification for Cytotoxic Peptides - Figure 1
- Notice Date
- 4/3/2018
- Notice Type
- Special Notice
- NAICS
- 238990
— All Other Specialty Trade Contractors
- Contracting Office
- Department of Energy, Lawrence Livermore National Laboratory (DOE Contractor), Industrial Partnerships & Commercialization, 7000 East Avenue, L-795, Livermore, California, 94550
- ZIP Code
- 94550
- Solicitation Number
- FBO376-18
- Archive Date
- 5/4/2018
- Point of Contact
- Connie L Pitcock, Phone: 925-422-1072
- E-Mail Address
-
pitcock1@llnl.gov
(pitcock1@llnl.gov)
- Small Business Set-Aside
- N/A
- Description
- Protease-Resistant Protein cages in Cell-Based Systems Opportunity : Lawrence Livermore National Laboratory (LLNL), operated by the Lawrence Livermore National Security (LLNS), LLC under contract no. DE-AC52-07NA27344 (Contract 44) with the U.S. Department of Energy (DOE), is offering the opportunity to participate in collaborative research and development and license intellectual property rights for commercialization of LLNL's method for improved expression and purification of cytotoxic peptides using engineered, protease-resistant protein cages in cell-based systems. Background : Antimicrobial peptides (AMPs) are strong therapeutic candidates against antibiotic -resistant, pathogenic bacteria, but they are difficult to produce in cell-based systems in sufficient quantities because they are cytotoxic and susceptible to proteolytic degradation. They are often chemically synthesized using liquid and/or solid phase peptide synthesis, which can be very expensive particularly for longer length peptides and suffer from additional disadvantage of limited yields. Alternatives such as cell-free protein synthesis systems (cell free expression, www.lifetechnologies.com ) are also expensive due to expensive raw materials and usually provide lower yields compared to in vivo (e.g., E. coli ) production systems. Description : Researchers at LLNL have developed a novel method to express and purify significant quantities of AMPs. AMP is fused to the N-terminus of a self-assembling protein called encapsulin from Thermotoga maritima, which forms protein cages with 60 monomer units. N-terminal fusion of the peptide to encapsulin results in encapsulation of the peptide within the protein cage, which prevents cytotoxicity of the peptide to the host and protects the peptide from host proteolysis, ultimately enabling high cellular production levels. In order to isolate the peptide from the protein cage, specific protease cleavage sites (e.g., TEV protease sites) are engineered into the encapsulin cage. Upon treatment with the appropriate protease, the peptide is released and can be isolated for a designated purpose. For additional technical information refer to the article " Re-directing bacterial microcompartment systems to enhance recombinant expression of lysis protein E from bacteriophage ϕX174 in Escherichia coli " Advantages : LLNL's proprietary method enables expression of peptides within encapsulin protein cages in an E. coli host-based expression system. The cages prevent toxicity of the peptide to the host organism as well as protect the peptide against non-specific proteases, thus enabling high peptide production levels. This system also has high fidelity compared to chemical synthesis and therefore may reduce downstream purification costs. Potential Applications •1) 1) Production and isolation of toxic peptides from a cell-based expression system; •2) 2) Production and isolation of protease-sensitive peptides from a cell-based expression system; •3) 3) Drug delivery of encapsulated peptides for therapeutic applications Development Status: LLNL has filed for patent protection for this technology: U.S. Patent Application 15/178454, "Engineering Bacterial Systems to Shield Toxicity During Non-Native Protein Expression and Purification " (LLNL internal case #IL-13008) U.S. Provisional Application 62/598984, "Engineered microcompartment protein and related methods and systems of engineering bacterial systems for non-native protein expression and purification" (LLNL internal case #IL-13262). 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 IPO website at https://ipo.llnl.gov/resources 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 method for improved expression and purification for cytotoxic peptides technology 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 Innovation and Partnerships Office P.O. Box 808, L-795 Livermore, CA 94551-0808 Attention: FBO 376-18 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 method for improved expression and purification for cytotoxic peptides technology.
- Web Link
-
FBO.gov Permalink
(https://www.fbo.gov/spg/DOE/LLNL/LL/FBO376-18/listing.html)
- Record
- SN04875658-W 20180405/180403231121-4a7a01c7aed00cde0d0449cc518d1720 (fbodaily.com)
- Source
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