报告时间：2014年6月12日（星期四）15:40

报告地点：龙赛理科楼南楼210报告厅

报告人：Prof. Bradley Olsen

报告人简介：

Bradley Olsen is the Paul M. Cook Career Development Assistant Professor in the Department of Chemical Engineering at MIT. He earned his S.B. in Chemical Engineering at MIT, his Ph.D. in Chemical Engineering at the University of California–Berkeley, and was a postdoctoral scholar at the California Institute of Technology. He started as an assistant professor at MIT in December 2009. Olsen’s research expertise is in materials chemistry and polymer physics, with a particular emphasis on molecular self-assembly, block copolymers, polymer networks and gels, and protein biomaterials. He has been recognized with a Hertz Fellowship, Tau Beta Pi Fellowship, Beckman Postdoctoral Fellowship, NIH Postdoctoral Fellowship, the American Physical Society Division of Polymer Physics/UK Polymer Physics Group Exchange Lectureship for Young Investigators, an NSF CAREER award, the Air Force Young Investigator Award, and a Sloan Fellowship.  Recently, he was also awarded the Chemical Engineering Graduate Teaching Award at MIT for his course on statistical mechanics.

报告摘要：

Protein-based materials show a great deal of potential as catalysts, sensors, and optoelectronics, where the unique efficiency, selectivity, or activity of enzymes can be captured to improve the performance of these devices. Control over the structure and orientation of the protein in three dimensions is required to improve transport through the devices, increase the density of active sites, and optimize the stability of the protein.  We demonstrate self-assembly of globular protein-polymer conjugates and fusion proteins into nanostructured phases as an elegant and simple method for structural control in biomaterials.  These conjugates or fusions may be conceptualized as diblock copolymers, where the first block is the globular protein and the second block is the synthetic polymer or coil-like protein sequence. These results begin to lay a foundation for understanding the general principles of self-assembly in block copolymers containing globular proteins.

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