Application of artificial backbone connectivity in the development of metalloenzyme mimics

Metal-dependent enzymes are abundant and vital catalytic agents in nature. The functional versatility of metalloenzymes has made them common targets for improvement by protein engineering as well as mimicry by de novo designed sequences. In both strategies, the incorporation of non-canonical cofacto...

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Bibliographic Details
Published inCurrent opinion in chemical biology Vol. 81; p. 102509
Main Authors Wolfe, Jacob A., Horne, W. Seth
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 01.08.2024
Subjects
Foldamers
Metalloenzymes
Proteomimetics
Metalloenzymes
Foldamers
Proteomimetics
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Summary:Metal-dependent enzymes are abundant and vital catalytic agents in nature. The functional versatility of metalloenzymes has made them common targets for improvement by protein engineering as well as mimicry by de novo designed sequences. In both strategies, the incorporation of non-canonical cofactors and/or non-canonical side chains has proved a useful tool. Less explored—but similarly powerful—is the utilization of non-canonical covalent modifications to the polypeptide backbone itself. Such efforts can entail either introduction of limited artificial monomers in natural chains to produce heterogeneous backbones or construction of completely abiotic oligomers that adopt defined folds. Herein, we review recent research applying artificial protein-like backbones in the construction of metalloenzyme mimics, highlighting progress as well as open questions in this emerging field. [Display omitted]
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ISSN:1367-5931
1879-0402
1879-0402
DOI:10.1016/j.cbpa.2024.102509