KOSEN 한인과학기술자네트워크

Bioengineered Proteins for Chemical/Biological Defense, Protection, and Decontamination Primary Sponsor: Department of Defense Deadline: 4/11/2001 KEYWORDS TECHNOLOGY AREAS: Chemical/Bio Defense, Human Systems OBJECTIVE: To develop an innovative, very high yield system for the production of unmodified recombinant proteins for use in chemical/biological (CB) decontamination and protection regimens, CB detection devices, and in the production of specially bioengineered protein-based materials for applications in bioinformatics, nanostructures, etc. DESCRIPTION: Numerous applications are being developed for proteins that have been engineered for specific biological or physical properties. The specificity of enzyme proteins in destroying or modifying various CB threats make them ideal choices for utilization in detection, protection, and decontamination devices. While the versatility and utility of such proteins is widely recognized, there are severe constraints in the production of the genetically modified proteins. Most protein production systems currently use laboratory "friendly" organisms that were selected not because of their utility in scaled-up fermentation processes but because they were convenient organisms for which there was much laboratory experience in their genetic and growth characterizations. This STTR seeks innovative and creative approaches to develop a high yield gene expression system that would allow the production of abundant amounts of bioengineered proteins under simple and comparatively inexpensive culturing conditions. This would generate adequate supplies of specialized proteins for utilization in CB defense and in the construction of protein-based biomaterials. PHASE I: This effort will focus on the analysis of systems that have the capabilities for producing high levels of proteins under minimal growth conditions in industrial-scale fermentations; e.g., yeast, fungi, bacteria, plants, and animal cultures. A successful Phase I will investigate and demonstrate approaches in the university and small business community that could be used for producing high protein yields and genetic constructions for recombinant proteins into those organisms. Protein yields, stability of the introduced genes, ease of preparation of proteins and cost of production of the proteins would all be factors to determine a suitable high-volume recombinant gene expression system. PHASE II: The small business should implement the scale-up of the culture system and yields of model recombinant proteins. Calculations of the cost of the high-yield proteins should be made to affirm the utility of the model system. Recommendations for the optimal cultural conditions should also be made. PHASE III DUAL USE APPLICATIONS: The system to be developed would significantly impact the development of devices for CB and nanotechnological applications and biomaterials for military applications, as well as a myriad of civilian, industrial and medical applications. Proteins that could be produced by the system include organophosphate-degrading enzymes for protection and decontamination, biochemical sensors, and very high purity blood proteins for remediating massive exsanguination. OPERATION AND SUPPORT COST (OSCR) REDUCTION: Operating and Support Costs (O&S) would be favorably impacted by this technology. A high-yield fermentation for bioengineered proteins would allow the current protein-based systems to be replaced by cheaper and more efficient protein expression systems. Furthermore, with the availability of abundant amounts of genetically modified proteins numerous other military and civilian applications would be accelerated. REFERENCES: 1. Rozkov, A., and Envors, S-O. 1999. Stabilization of a proteolytically sensitive cytoplasmic recombinant protein during transition to downstream processing. Biotechnology. Bioengineering. 62, 730-738. 2. Mukhopadhyay, A. 1997. Inclusion bodies and purification of proteins in biologically active form. Adv. Biochem. Eng./Biotechnol. 56, 61-109. 3. Vieth, W.R. 1994 Bioprocess engineering. J. Wiley and Sons. 4. Shuler, M.L., and Kargi, F. 1992. Bioprocess engineering. Prentice Hall. KEYWORDS: Microbial high-yield protein systems; bioengineered proteins; recombinant proteins; protein purification. DoD Notice: Between January 2 and February 28, 2001, you may talk directly with the DoD scientists and engineers who authored the solicitation topics, to ask technical questions about the topics. The Topic Author is listed in the box below. For reasons of competitive fairness, direct communication between proposers and topic authors is not allowed after February 28, 2001, when DoD begins accepting proposals under this solicitation. Technical Point of Contact: Leo W. Parks Phone: 919-549-4325 Fax: 919-549-4399 Email: ParksLW@arl.aro.army.mil 2nd Technical Point of Contact: Micheline K. Strand Phone: 919-549-4343 Fax: 919-549-4399 Email: StrandMK@arl.aro.army.mil After February 28, 2001 proposers may still submit written questions about solicitation topics through the SBIR/STTR Interactive Topic Information System (SITIS). If you have general questions about DoD SBIR program, please contact the DoD SBIR Help Desk at (800) 382-4634 or email to SBIRHELP@teltech.com. NOTE: The Solicitations listed on this site are copies from the various SBIR agency solicitations and are not necessarily the latest and most up-to-date. For this reason, you should use the agency link listed below which will take you directly to the appropriate agency server where you can read the official version of this solicitation and download the appropriate forms and rules. The official link for this solicitation is: http://www.acq.osd.mil/sadbu/sbir/sttr01/dod_sttr01.htm. DoD will begin accepting proposals on March 1, 2001. The solicitation closing date is April 11, 2001.