369062 Polypeptoids As Model Systems for Understanding Biopolymer Self-Assembly

Monday, November 17, 2014: 8:30 AM
International 10 (Marriott Marquis Atlanta)
Rachel Segalman, Departments of Materials and Chemical Engineering, UCSB, Santa Barbara, CA, Ronald N. Zuckermann, Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA, Adrianne M. Rosales, Department of Chemical Engineering, University of California, Berkeley, Berkeley, CA, Hannah Murnen, Chemical Engineering, University of California, Berkeley, Berkeley, CA and Hilda Buss, Dept of Chemical Engineering, University of California, Berkeley, Berkeley, CA

Biological polymers, such as polypeptides, are responsible for many of life’s most sophisticated functions due to precisely evolved hierarchical structures. Protein structures are the result of monodisperse sequences of amino acids that fold into well-defined chain shapes and tertiary structures with a degree of complexity that is very difficult to understand.  Non-natural polymers offer the stability and robustness necessary for materials applications; however, our ability to control primary and secondary structure in these systems is comparatively crude. In addition, the relationship between monomer sequence and self-assembly is not well understood for biological molecules, much less synthetic polymers. Thus, there is a need to explore self-assembly phase space with sequence using a model system. Polypeptoids are non-natural, sequence specific polymers that offer the opportunity to probe the effect of sequence on self-assembly with much simpler molecular interactions and more scalable synthesis than traditional polypeptides.  In this talk, I will discuss the use of this model system to understand the role of sequence on chain collapse and globule formation in solution, polymer crystallization, and block copolymer self-assembly.  I will then discuss potential application as surface active agents for anti-fouling.

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