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Mimicking Cell Membranes with Polymers and Proteins Cellular membranes and their structures have been a topic

of interest for both biochemists and biomolecular engineers alike. With a unique lipid bilayer structure integrated with specialized proteins, cellular membranes are able to selectively control the flow of materials into and out of cells as well as interact with proteins and lipids in the surrounding environments. In order to take the functions of specific proteins out of their normal biological roles, new methods in using block copolymers have been utilized to mimic the environment of the lipid bilayer cellular membrane.1 The Kumar group at Penn State is conducting research on block copolymer synthesis and self-assembly to create biomimetic membranes. In particular, my research this summer would revolve around three different sets of copolymers: PB-PEO [poly(butadiene)-poly(ethylene oxide)], PEE-PEO [poly(ethylethylene)-poly(ethylene oxide)], and PI-PEO [poly(imide)-poly(ethylene oxide)]. These combinations of copolymers, when organized in solution, aggregate to form the familiar lipid bilayer similar to that of a cell membrane due to the hydrophilic-hydrophobic interactions between the polymers.1 To begin research on how different protein complexes interact with the block copolymer biomimetic membranes, the aquaporin protein from E. Coli (AqpZ) would be studied first. Aquaporins are unique protein complexes because they allow for the rapid movement of water across the membrane, and it is one of the most understood membrane proteins. In addition to AqpZ, a protein from sheep eye lenses (AOP0) would also be studied. The usefulness of this protein comes from the fact that it forms two-dimensional arrays, auseful form factor for membranes, and can be genetically engineered to grow in yeast cells, which makes it readily available. The study of these two proteins and their interactions with the block copolymer membranes would make up a large part of my summer research. In addition to these proteins, I would work with one of the Kumar groups graduate students on his project involving the interactions of the protein complex Photosystem I (PSI) with gold to create a current that can increase the production of hydrogen, which fuels energy production in photosynthetic organisms. PSI has the unique ability of aggregating into 2D crystals, which can easily be attached to a gold electrode to produce a current. The research involving block copolymers done early in the summer would come into play as the group tries to use block copolymers to further stabilize the PSI protein complex, thus increasing the current produced as well as hydrogen production.2 Block copolymers have direct application in the field of biochemical engineering by creating an environment that can mimic the membrane environment created by cells. These membranes have the ability to interact with many different proteins and even help stabilize large protein complexes to increase the production of energy. The research this summer and throughout my honors thesis work this fall would focus on the results of

Sean McCrea

these experiments as well as the applications of the results to future projects in a similar field. References 1. 2. Kumar, M, Maranas, J (2014) Directed design of polymer membranes for protein self-assembly. Saboe, P (2014) Photosynthetic membrane protein crystals for hydrogen production.

Sean McCrea