Abstract
Enzymes are predominantly proteins able to effectively and selectively catalyze highly complex biochemical reactions in mild reaction conditions. Nevertheless, they are limited to the arsenal of reactions that have emerged during natural evolution in compliance with their intrinsic nature, three-dimensional structures and dynamics. They optimally work in physiological conditions for a limited range of reactions, and thus exhibit a low tolerance for solvent and temperature conditions. The de novo design of synthetic highly stable enzymes able to catalyze a broad range of chemical reactions in variable conditions is a great challenge, which requires the development of programmable and finely tunable artificial tools. Interestingly, over the last two decades, chemists developed protein secondary structure mimics to achieve some desirable features of proteins, which are able to interfere with the biological processes. Such non-natural oligomers, so called foldamers, can adopt highly stable and predictable architectures and have extensively demonstrated their attractiveness for widespread applications in fields from biomedical to material science. Foldamer science was more recently considered to provide original solutions to the de novo design of artificial enzymes. This review covers recent developments related to peptidomimetic foldamers with catalytic properties and the principles that have guided their design.
Highlights
Enzymes are incredible powerful catalysts, being typically non-toxic and environmentally friendly, while capable of performing remarkably difficult chemical transformations with relative ease, unmatched substrate, and product selectivity [1,2,3]
We mainly focus on the potential of peptidomimetic foldamers including, among others, β- and γ-peptides, peptoids and oligoureas peptides for organocatalysis
Such a conjugation process allows for the creation of hybrid catalysts with new features resulting from the combination of the molecular recognition properties of the folded molecule with the inherent activity of the adjunct catalytic center
Summary
Enzymes are incredible powerful catalysts, being typically non-toxic and environmentally friendly, while capable of performing remarkably difficult chemical transformations with relative ease, unmatched substrate, and product selectivity [1,2,3] As such, they offer many opportunities in chemical industry, their intrinsic vulnerabilities related to their low thermal stability, low tolerance for solvent conditions, as well as their poor diversity of substrates and their high cost of production, seriously hamper their attractiveness. Foldamers provide an infinite range of scaffolds for presenting complex sets of functional groups to reproduce the structure and function of biomacromolecules, making them attractive for broad applications ranging from nanotechnology to biomedical fields, biopolymer surface recognition and nanomaterials These areas are well covered in reviews [29,30,31,32,33]. We describe how a strict control of the topology could serve the design of biomimetic catalysts
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