Highly stable and tunable peptoid/hemin enzymatic mimetics with natural peroxidase-like activities

作者：Tengyue Jian, Yicheng Zhou, Peipei Wang, Wenchao Yang, Peng Mu, Xin Zhang, Xiao Zhang, Xiao Zhang, Xiao Zhang, Chun‐Long Chen · 发表于：Nature Communications · 年份：2022 · DOI：10.1038/s41467-022-30285-9 · 被引用次数：98 · 研究领域：Chemical Synthesis and Analysis、Enzyme-mediated dye degradation、Sulfur-Based Synthesis Techniques

Abstract Developing tunable and stable peroxidase mimetics with high catalytic efficiency provides a promising opportunity to improve and expand enzymatic catalysis in lignin depolymerization. A class of peptoid-based peroxidase mimetics with tunable catalytic activity and high stability is developed by constructing peptoids and hemins into self-assembled crystalline nanomaterials. By varying peptoid side chain chemistry to tailor the microenvironment of active sites, these self-assembled peptoid/hemin nanomaterials (Pep/hemin) exhibit highly modulable catalytic activities toward two lignin model substrates 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 3,3’,5,5’-tetramethylbenzidine. Among them, a Pep/hemin complex containing the pyridyl side chain showed the best catalytic efficiency ( V max / K m = 5.81 × 10 −3 s −1 ). These Pep/hemin catalysts are highly stable; kinetics studies suggest that they follow a peroxidase-like mechanism. Moreover, they exhibit a high efficacy on depolymerization of a biorefinery lignin. Because Pep/hemin catalysts are highly robust and tunable, we expect that they offer tremendous opportunities for lignin valorization to high value products.