An Automatic Learning Gesture Recognition Interface for Dismounted Soldier Training Systems

Recombinant expression of human proteins is a potentially valuable method for large scale production of hemostatic materials. However, manufacturing-scale production using traditional recombinant DNA techniques is problematic due to the low yield ofactive protein and complex purification. We propose to utilize a novel technique to produce hemostatic human proteins in bacteria and mammalian cells from completely synthetic genes designed in the computer. The approach is based on the complete chemicalsynthesis of large DNA molecules encoding fibrinogen a, b and g subunits and modified versions of these genes produced as an array of component oligonucleotides that are then assembled, ligated and expressed in E. coli. This approach is enabled byinexpensive high-throughput oligonucleotide array synthesis developed by Egea Biosciences that allows complete customization of the protein/vector/expression system. To maximize expression, synthetic genes have been designed using E. coli, yeast ormammalian preferred codons to increase protein expression as well as specific sequences to enable high efficiency protein purification. In Phase I of this project, synthetic genes for recombinant fibrinogen subunits were designed, constructed andexpressed. Phase II of this project will continue and expand this strategy to create over 1000 variant hemostatic proteins, screen these for stability and activity, and maximize expression in bacterial and mammalian hosts. The re-engineeredgene/vector/host combination will be a platform for further sequence alterations to maximize protein expression and enable large-scale manufacturing. Artificial gene design, construction and expression will be explored for the production of recombinantactive fibrinogen and other hemostatic proteins for commercial use in