Synthesis of Polymer-Protein Hybrid Materials Using Site Selective Protein Modification Reactions

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In this project funded by the Macromolecular, Supramolecular and Nanochemistry Program of the Chemistry Division, Matthew Francis of the University of California at Berkeley will develop a scalable N-terminal transamination reaction as a means to modify proteins with a single functional group at a single location and to demonstrate the use of this methodology in the preparation of protein-polymer hybrids for water purification. The approach to the project involves two parts. First, the PI's recently developed N-terminal chemical modification reaction will be used to attach polymers that exhibit a lower critical solution temperature (LCST) to proteins capable of sequestering heavy metals, actinides or hormones. The efficacy of these protein-polymer hybrids in removing trace amounts of these contaminants from water will be studied. Second, new low-cost, efficient transamination reagents will be developed based upon yield improvement of the parent transamination chemistry, imine capture via quinine condensation, or adaptations of the Claisen condensation. It is thought that such methods will improve the scalability of the protein modification chemistry and thereby facilitate manufacturing and innovation with these protein-polymer systems. The broader impacts involve training graduate and undergraduate students, outreach to adult learners through presentations at Rotary Club meetings and other such local organizations, creating a new "Chemistry in the Kitchen" class, and the potential societal benefits of methodologies to target and remove specific impurities from water.The new techniques developed in this work will provide many avenues for the modification of biomolecules in specific locations. These modified proteins could be used in a variety of biotechnology applications including low cost agents for the removal of heavy metal ions, actinide metals, and organic toxins from drinking water.