Research

Current Projects

We use controlled radical polymerization (also known as living radical polymerization or reversible deactivation radical polymerization) to create precisely defined polymers for materials applications. We apply precision polymers to ongoing challenges in polymer sustainability and biomaterials including:

Dynamic networks that can facilitate reprocessing of thermosets
Mild conditions for polymerizaiton under light and polymer degradation under UV.
Tailoring polymer properties over time using chemical fuels.
Biological applications including protein-polymer bioconjugates.
Polymers that self assemble with lipids for stable and effective environments for membrane protein studies.

Photochemistry and Precision Polymer Synthesis

We are interested in using photochemistry to polymerize various monomers since this gives both control over WHERE and WHEN the polymerization is occurring. Our group is particularly interested in using photochemistry under relatively mild conditions such as using sunlight and mild light sources to tailor make polymers for various applications.

Ongoing Projects involve use of light to degrade polymers. This has important applications ranging from 3D printing to end of life for plastics. We also look for universal descriptions of photopolymerization processes that aid both photopolymerization and photodegradation.

Dynamic Materials

Dynamic bonds are those that are able to associate, dissociate or exchange, either intrinsically or upon external stimulus. Dynamic bonds also can lead to materials with increased mechanical properties, toughness, energy dissipation mechanisms, etc. Networks with dynamic, or reversible bonds can form self-healing materials by reforming the bonds after they are initially ruptured by the external force. Self-healing polymer networks are materials which can be damaged through scratches, cuts or fractures and reform into a "healed" structure after the appropriate stimulus is applied.

Our group is examining the effects of different dynamic bonding units on the properties of the self-healing materials.

Ongoing projects use these dynamic materials for composite applications, and towards more sustainable uses of poylmers including reprocessable thermosets and adaptable adhesives in 3D printing.

Fuelled and Out of Equilibrium Materials

We are inspired by biological systems that use chemical fuels to drive complex reactions that lead to macroscopic changes in materials, such as muscle movement and transport of materials. We aim to develop responsive abiotic materials that change and respond to chemical fuels. These can be phase changes, or mechanical properties that change under fuelling.

Ongoing projects focus on driving changes in materials properties in various soft materials structures.

Lipid Polymer Nanodiscs for Membrane Proteins

Membrane proteins comprise approximately 1/3 of the genome, yet their structures are much less well understood than water soluble proteins. Using precision polymerization we have developed polymers that self assemble with lipids to form well defined nanodiscs. WIth our biochemistry/biophysics collaborators we have shown that these nanodiscs form excellent environmetns that closely match the native bilayer, but facilitate structural studies.

Ongoing projects involve development of more biocompatible polymers, and ongoing studies in the interactions between the membrane proteins and the lipid nanodiscs.

Protein-Polymer Hybrids

Understanding protein function and structure is a fascinating part of modern biochemistry. With the development of controlled radical polymerization it has become possible to synthesize well defined protein-polymer hybrids.

These protein-polymer hybrids consist of a naturally occurring protein, covalently linked to one or more synthetic polymers. The advantages of the protein-polymer hybrid are that the polymer can stabilize the protein against environmental and biological stressors.

Ongoing projects focus on protein-polymer hybrids and studies the effect of polymer structure and architecture on the stability and function on the protein using state of the art NMR methods.

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