Nature's proteins are linear, sequence-controlled copolymers built of a versatile library of 21 amino acids. The precise, tailored structures attained by proteins in solution allow them to achieve an unparalleled degree of functional perfection. These perfect structures are a product of billions of years of biological evolution, a process that is an impractical target for direct emulation by chemists. A variety of combinatorial/parallel synthesis approaches have been reported in the literature as a means of easy access to a range of rationally- and semi-rationally designed macromolecular architectures. By necessity, many of these approaches are limited to relatively well-behaved, structurally simple monomers.<br/><br/>Here, we present a pathway to well-defined unimolecular micelles built from copolymers incorporating superhydrophobic (fluorous) and superhydrophilic poly(ethyleneglycol) (PEG) monomers. The polymers were prepared by ring-opening metathesis polymerization (ROMP), a methodology that is remarkably tolerant to a variety of functional groups and electronic properties of the monomers. The polymer library has been characterized by a number of imaging techniques. Even in the absence of perfect sequence control, we were able to achieve a narrow distribution of the hydrodynamic radii of the micelles, as well as separation of the co-monomers into well-defined microphases. This approach is general, and can be applied to the design of macromolecular architectures tailored for oxygen transport, catalysis, and nanocasting of porous catalyst supports.

Synthesis of macromolecular architectures with a high hydrophobic/hydrophilic contrast by ring-opening metathesis polymerization

249th National Meeting (2015)

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