Self‐assembled Peptide‐based Biocatalyst

Enzymatically elegant characteristics and functions of many natural intracellular pathways pique people's curiosity in both solving the deep natural mystery and creating cutting-edge materials for environmental sustainability. However, enzymes such as oxidoreductases, hydrolases, transferases, lyases, isomerases, ligases, and translocases are usually unstable and full of complexity in enzymatic reactions. Thus, there is an urgent need to develop biomimetic enzymes that are simple with increased stability. In this chapter, we focus on supramolecular peptide-based catalysts. These biocatalysts are constructed by noncovalent interactions, including hydrogen-bonding, hydrophobic interactions, electrostatic interactions, and Van der Waals interactions. A naturally occurring enzyme is made up of a protein and partly ribonucleic acid. Amino acids and peptides are main constituents of proteins. They could work as alternative building blocks when designing new biocatalysts. When peptide-based catalysts are used as fundamental cellular component, it is possible to control their structures and final catalytic capacities due to their distinct characteristics such as selectivity and autocatalysis. In this chapter, we also pay attention on how to choose assembled peptide building blocks, regulate their functionality, achieve catalytic reactions, and illustrate their catalytic mechanisms in a variety of catalytic processes. Finally, we hope that the results presented in this chapter can inspire readers to design novel peptide-based catalysts with high selectivity and catalytic performance.