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Research
Many of the current and future challenges that chemistry hopes to address require molecules of ever-increasing complexity. We are synthetic chemists guided by how Nature uses the process of evolution to arrive at remarkably sophisticated biomolecules. Our approach involves creating synthetic molecules that harness self-assembly and structural permutation to generate complex materials that can continue to evolve. While synthetic peptides hold immense potential for this purpose, they are underutilized in organic, inorganic, and materials chemistry. Our group aims to unlock the versatility of peptides to craft advanced, multifunctional materials serving as catalysts, sorbents, and scaffolds for biomimetic chemistry.
Porous Peptide Frameworks
Porous crystalline frameworks have 3-D microenvironments that are widely useful in industrial separation and catalytic processes. More advanced frameworks (e.g. metal–organic frameworks) are being actively explored to address challenges in sustainable chemistry. Our group has developed peptides as general building blocks to make frameworks with pore structures approaching the sophistication of protein active sites, The long-term goal of this research area is to develop predictable strategies for making porous peptide frameworks. The objective is to synthesize frameworks with protein-like environments to enhance separations and catalysis, exploring fundamental structure-function relationships.
Evolvable Catalysts
Homogeneous metal complexes have proven to be powerful catalysts for numerous applications ranging from small-molecule transformation to organic synthesis. However, slight inaccuracies in "rational" design of catalysts can manifest as drastic reduction in catalysis rate and selectivity. We propose that applying the process of evolution to synthetic systems can lead to highly effective catalyst generation. Sequence-defined oligomers are ideal candidates to build such catalysts due to their modular and efficient assembly, while their sequence-defined nature facilitates the process of variation and selection.
Excision of Metalloenzyme Active Sites
Non-heme Fe and Cu-based oxygenases perform exceptionally challenging oxygenations vital for human health. These enzymes are difficult to study and model, and as a result, the structural basis for their extraordinary reactivity is not fully known. We aim to replicate metalloprotein active sites using single-crystalline peptide frameworks, which is expected to stabilize fleeting species and allow for immediate characterization by X-ray crystallography. This general strategy is expected to yield valuable mechanistic and structural details not readily obtainable otherwise.
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