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Review

Catalytic Foldamers: When the Structure Guides the Function

1
IBMM, Université de Montpellier, CNRS, ENSCM, 34093 Montpellier, France
2
Institute of Regenerative Medicine and Biotherapies, CARTIGEN, CHU Montpellier, 34090 Montpellier, France
*
Author to whom correspondence should be addressed.
Catalysts 2020, 10(6), 700; https://doi.org/10.3390/catal10060700
Received: 28 May 2020 / Revised: 16 June 2020 / Accepted: 18 June 2020 / Published: 22 June 2020
(This article belongs to the Special Issue Organocatalysis: Advances, Opportunity, and Challenges)
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. View Full-Text
Keywords: foldamer; peptidomimetic; cooperation; organocatalyst foldamer; peptidomimetic; cooperation; organocatalyst
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MDPI and ACS Style

Legrand, B.; Aguesseau-Kondrotas, J.; Simon, M.; Maillard, L. Catalytic Foldamers: When the Structure Guides the Function. Catalysts 2020, 10, 700. https://doi.org/10.3390/catal10060700

AMA Style

Legrand B, Aguesseau-Kondrotas J, Simon M, Maillard L. Catalytic Foldamers: When the Structure Guides the Function. Catalysts. 2020; 10(6):700. https://doi.org/10.3390/catal10060700

Chicago/Turabian Style

Legrand, Baptiste; Aguesseau-Kondrotas, Julie; Simon, Matthieu; Maillard, Ludovic. 2020. "Catalytic Foldamers: When the Structure Guides the Function" Catalysts 10, no. 6: 700. https://doi.org/10.3390/catal10060700

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