1. Academic Validation
  2. Supramolecular enzyme-mimicking catalysts self-assembled from peptides

Supramolecular enzyme-mimicking catalysts self-assembled from peptides

  • iScience. 2022 Dec 20;26(1):105831. doi: 10.1016/j.isci.2022.105831.
Qing Liu 1 Akinori Kuzuya 1 Zhen-Gang Wang 2
Affiliations

Affiliations

  • 1 Department of Chemistry and Materials Engineering, Kansai University, Yamate-cho 3-3-35, Suita, Osaka 564-8680, Japan.
  • 2 State Key Laboratory of Organic-Inorganic Composites, Key Lab of Biomedical Materials of Natural Macromolecules (Beijing University of Chemical Technology, Ministry of Education), Beijing Laboratory of Biomedical Materials, College of Materials Science and Engineering, Beijing University of Chemical Technology, Beijing 100029, China.
Abstract

Natural enzymes catalyze biochemical transformations in superior catalytic efficiency and remarkable substrate specificity. The excellent catalytic repertoire of enzymes is attributed to the sophisticated chemical structures of their active sites, as a result of billions-of-years natural evolution. However, large-scale practical applications of natural enzymes are restricted due to their poor stability, difficulty in modification, and high costs of production. One viable solution is to fabricate supramolecular catalysts with enzyme-mimetic active sites. In this review, we introduce the principles and strategies of designing peptide-based artificial enzymes which display catalytic activities similar to those of natural enzymes, such as aldolases, laccases, peroxidases, and hydrolases (mainly the esterases and phosphatases). We also discuss some multifunctional enzyme-mimicking systems which are capable of catalyzing orthogonal or cascade reactions. We highlight the relationship between structures of enzyme-like active sites and the catalytic properties, as well as the significance of these studies from an evolutionary point of view.

Keywords

Biomolecules; Chemistry; Peptides; Supramolecular chemistry.

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