Self-assembly of the de novo designed peptides to produce supramolecular catalysts with built-in enzyme-like active sites: a review of structure–activity relationship

Enzymes have been widely applied for green transformation in a variety of fields due to their remarkable catalytic properties, which are largely attributed to the spatial arrangement of the essential functional groups in the enzymatic active structures. The formation of the elegant active sites is a result of the three-dimensional protein folding, which has been screened by billions of years’ nature evolution. This poses the challenge in building the enzyme-like active sites into the artificial catalysts, which are designed aiming to rival native enzymes in the catalytic efficacy. De novo designed peptides have been employed as the building blocks to self-assemble into enzyme-mimicking catalysts by configuring their side chain groups to form a catalytically active pocket. This review discusses the progress in the peptides-based supramolecular catalysts that show aldolase-, hydrolase-, oxidase-like activities; focuses on the structure–activity relationship of the active sites; and outlooks the possible future directions of the supramolecular catalysts.