Chun-Long Chen1,2
Pacific Northwest National Laboratory1,University of Washington2
Chun-Long Chen1,2
Pacific Northwest National Laboratory1,University of Washington2
While natural enzymes, including lignin peroxidase, phosphotriesterase, and carbonic anhydrase, are promising for various applications, such as lignin depolymerization, degradation of toxic organophosphates, and accelerated CO<sub>2</sub> precipitation, there are numerous key technical barriers to prevent their practical applications, because they often suffer from low stability and high cost. To circumvent these barriers, researchers have started to develop synthetic materials as enzyme mimetics with enhanced stability for various purposes. Despite tremendous efforts made in this area, constructing highly efficient and robust enzyme mimetics with natural enzyme-like flexibility in tuning active sites and microenvironments remains a grand challenge.<br/><br/>In this presentation, we will report our recent progress in developing peptoid-based crystalline nanomaterials as highly robust and programmable catalysts for a variety of applications. Peptoids are one of the most advanced classes of sequence-defined synthetic foldamers that bridge the properties of proteins and polymers.<sup> 1-4</sup> While exhibiting protein- and peptide-like molecular recognition, peptoids offer unique opportunities for controlled synthesis of hierarchically-structured crystalline nanomaterials<sup>1,5-7</sup> exclusively through side-chain chemistry due to the lack of backbone hydrogen bond donors. Because of highly tunable features and robustness of these peptoid-based crystalline nanomaterials, they provide an ideal platform to mimic nature enzymes by offering high surface area, programmable microenvironments, and other unique advantages. For example, comparing to a typical lignin peroxidase which contains one active site per enzyme molecule, peptoid-based crystalline nanotube catalysts can accommodate a high-density of active sites to achieve a significantly enhanced catalytic activity in lignin depolymerization.<sup> 8</sup> Moreover, due to their high chemical and thermal stability, these peptoid-based catalysts can be operated at a variety of conditions, such as at elevated reaction temperature and broad pH range which nature enzymes denature.<br/><br/>References<br/>1. Sun et al., <i>ACS Nano</i> <b>7</b>, 4715-4732 (2013); 2. Shao et al., <i>Chem. Rev.</i> <b>122</b>, 17397-17478 (2022); 3. Li et al., <i>Chem. Rev.</i> <b>121</b>, 14031-14087 (2021); 4. Cai et al., <i>Acc. Chem. Res.</i> <b>54</b>, 81-91 (2021); 5. Jin et al., <i>Nature Comm. </i><b>9</b>, 270 (2018); 6. Jin et al., <i>Nature Comm.</i> <b>7</b>, 12252 (2016); 7. Wang et al., <i>Science Adv. </i><b>7</b>, eabg1448 (2021); 8. Jian et al., <i>Nature Comm. </i><b>13</b>, 3025 (2022).