Designing macromolecular materials with functions inspired by biological systems.

Rational design of biomimetic copolymers

Natural biomacromolecules possess remarkably complex functions, but their inherent instability hinders their applications in cutting-edge materials. Enter amphiphilic polymers—a class of materials that share similarities with proteins in terms of size and shape. These polymers offer a captivating complement to proteins, exhibiting enhanced chemical diversity and robustness across a range of conditions. Leveraging a combination of systematic studies guided by rational design and regression-guided optimization, we are uncovering the fundamental design principles governing hierarchical structures. From catalysis to industrial separations, these newfound principles pave the way for transformative advancements.

Peptide-polymer amphiphiles

Self-assembled morphologies create confined and ordered environments that can be leveraged in energy and health applications including green catalysis, mineralization of critical materials, and therapeutics. Peptide polymer amphiphiles (PPAs) are self-assembling materials that leverage the function and specificity of peptides with the stability and diversity of synthetic polymers. The Knight lab has played a pioneering role in developing oligomeric peptide-polymer assemblies through 1) mapping the morphological space as a function of polymer and peptide properties in addition to 2) investigating how fundamental polymer properties drive nonequilibrium assemblies. Currently, we are focused on developing materials with functional peptides with applications in antibiotics and catalysis.

Connection primary sequence to conformation

The precise sequences found in biomacromolecules grant them a remarkable range of biological functions. However, achieving the same level of structural control at the monomer level for synthetic materials has proven to be a persistent challenge. To address this, we adopt a systematic approach that begins by defining the relationships between sequence and structure in synthetic polymers. Subsequently, we aim to establish connections between these structures and the emergence of desired functionalities including the development of macromolecular therapeutics. Peptoids, which are oligomers of N-substituted glycine, serve as sequence-defined synthetic polymers that facilitate the exploration of sequence-to-property relationships. Our research has yielded innovative methods for the high-throughput characterization of peptidomimetic polymers, utilizing environmentally sensitive dyes, machine-learning-based image analysis, and MALDI sequencing.

DNA-directed assembly of block copolymers

Screening libraries of biomacromolecules has achieved remarkable breakthrough through techniques like directed evolution. However, the exploration of synthetic polymers has been constrained in comparison. To unlock the vast design potential encompassing, size, composition, and architecture, we have devised a DNA-based strategy. This strategy enables the rapid and efficient coupling of polymer building blocks, generating large libraries of biohybrid block copolymers. Through this platform, we aim to unravel the intricate structure-to-property relationships within this new class of polymer materials and harness their potential in therapeutic applications.