Block Copolymer-Based Biomembranes Functionalized with Energy Transduction Proteins
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Block Copolymer-Based Biomembranes Functionalized with Energy Transduction Proteins Dean Ho, Benjamin Chu, Hyeseung Lee, Karen Kuo, and Carlo D. Montemagno Department of Bioengineering, University of California, Los Angeles Los Angeles, CA 90095,U.S.A.
ABSTRACT Block copolymer-based membranes can be functionalized with energy transducing proteins to reveal a versatile family of nanoscale materials. Our work has demonstrated the fabrication of protein-functionalized ABA triblock copolymer nanovesicles that possess a broad applicability towards areas like biosensing and energy production. ABA triblock copolymers possess certain advantages over lipid systems. For example, they can mimic biomembrane environments necessary for membrane protein refolding in a single chain (hydrophilic(A)hydrophobic(B)-hydrophilic(A)), enabling large-area membrane fabrication using methods like Langmuir-Blodgett (LB) deposition. Furthermore, the robustness of the polymer molecules/structure result in spontaneous and rapid protein-functionalized nano-vesicle formation that retains structure as well as protein functionality for up to several months, compared to one to two weeks for the lipid systems (e.g. POPC). The membrane protein, Bacteriorhodopsin (BR), found in Halobacterium Halobium, is a light-actuated proton pump that develops gradients towards the demonstration of coupled functionality with other membrane proteins, such as the production of electricity through Bacteriorhodopsin activity-dependent reversal of Cytochrome C Oxidase (COX), found in Rhodobacter Sphaeroides. Proteinfunctionalized materials have the exciting potential of serving as the core technology behind a series of fieldable devices that are driven completely by biomolecules. INTRODUCTION Energy-transducing proteins remain at the forefront of the discussions of the applicability of biomolecules as a core technology for nanobiological devices in the areas of medicine, biofuel cells, and a wide variety of other fields. While conventional methods utilizing synthetic lipid membranes for protein functionality assays have yielded a plethora of information with respects to the basic biology of membrane protein behavior [1-4], robust materials for device fabrication has been a central motivation in functional material technology. This work focuses on the reconstitution of the energy-transducing proteins, Bacteriorhodopsin (BR), found in the Halobacterium Halobium, as well as Cytochrome C Oxidase (COX), from Rhodobacter Sphaeroides, into block copolymer-based biomimetic membranes comprised of PMOXAPDMS-PMOXA. While biomolecule evolution has cemented their place as perhaps the most efficient energy transducing machinery in existence, block copolymer biomimetic membranes signify a versatile class of nanostructured materials that can be used to harness membrane protein activity [5-7], yielding a plethora of application-specific materials towards the buildup of a multicomponent system that preserves inherent molecular function.
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EXPERIMENTAL DETAILS Protein pur
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