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C–H activation

Complex peptides made simple

Nature Chemistry volume 9, pages 9–10 (2017)Cite this article

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Nature oxidizes biosynthetic intermediates into structurally and functionally diverse peptides. An iron-catalysed C–H oxidation mimics this approach in the lab, enabling chemists to synthesize structural analogues with ease.

Naturally occurring peptides exhibit an extraordinary range of properties and biological activities1. Non-ribosomal peptides (NRPs) continue to represent an invaluable source of new small-molecule drugs2, having already provided antibiotics such as the β-lactam, glycopeptide and lipopeptide families3. Advances in the bioengineering of NRP synthases4 and the availability of non-proteinogenic amino acids have expanded the compound pool available to researchers in recent years, but chemical synthesis remains the tool of choice for the study of structural modifications on NRP derivatives nonetheless. Analogue synthesis is particularly laborious for structurally complex peptides when each one must be made from the ground up.

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Figure 1: Oxidative diversification of amino acids and peptides by small-molecule iron catalysis.

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Authors and Affiliations

  1. Sean Bartlett and David R. Spring are in the Department of Chemistry at the University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK,

    Sean Bartlett & David R. Spring

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  1. Sean Bartlett
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  2. David R. Spring
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Correspondence to David R. Spring.

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Bartlett, S., Spring, D. Complex peptides made simple. Nature Chem 9, 9–10 (2017). https://doi.org/10.1038/nchem.2701

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