University of Connecticut |
Polymer Program SeminarAssembling Nanoparticles, Viruses and Proteins into Nanostructured Materials Monday, February 4, 2008 11:00 am , IMS Room 20 The fabrication of functional nanostructured materials requires practical approaches to self-assembly on multiple length scales. In my graduate research, the assembly of nanoparticles at oil-water interfaces driven by reduction in interfacial energy was investigated. Studies on the dynamics of the nanoparticles and self-assembled structures formed at the interface, using fluorescence photobleaching methods and in situ small angle X-ray scattering, suggest a liquid-like behavior and ordering at the interface. Cross-linking of the nanoparticle assemblies with functional ligands, affords robust membranes that maintain their integrity even when they are removed from the interface. These composite membranes, nanometers in thickness, are elastic yet permeable. The assembly of viruses and other biological complexes at fluid interfaces was also investigated. These assemblies enable the potential use of bioparticles as natural supramolecular building blocks in materials with well-defined bio-functionalities. Although tremendous progress has been made in nanotechnology, nature still has much to teach us about the synthesis and integration of functional nanomaterials. For instance, many biological functions involve the formation of protein complexes, where multiple proteins work in a concerted manner. My current research focus is to engineer these protein based nanomaterials, with the aim of controlling their biological activity through artificial architecture. For example, a protein nanodevice with an allosteric control was designed, based on an engineered three-domain protein that can form a looped structure upon reaction with a small synthetic linker molecule. The change in overall protein conformation during the looping process, as evidenced by solution small angle X-ray scattering, alters the activity of the functional domain of the protein. Thus, this “loop”, provides a route to regulate a protein’s activity allosterically. Expanding this work should lead to novel protein-based responsive materials.
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