Enhancing Metal-binding with Noncanonical Coordinating Amino Acids

Authors

  • Luca Sauser Department of Chemistry, University of Zurich, Winterthurerstrasse 190, CH-8057, Zurich, Switzerland
  • Michal S. Shoshan Department of Chemistry, University of Zurich, Winterthurerstrasse 190, CH-8057, Zurich, Switzerland;, Email: michal.shoshan@chem.uzh.ch

DOI:

https://doi.org/10.2533/chimia.2021.530

Keywords:

Metal-binding, Noncanonical amino acids, Nonribosomal peptides, Peptide siderophores, Post-translational modifications

Abstract

More than 50% of proteinogenic amino acid sidechains can bind metal ions, enabling proteins and peptides to bear these ions as cofactors. Nevertheless, post-translational modifications and incorporation of noncanonical amino acids bestow peptides and proteins myriads of other coordination capabilities, thanks to an enhanced metal binding. Here we summarize selected examples of natural and artificial systems that contain one or more noncanonical amino acids coordinating a metal ion and subsequently achieve a new or enhanced function. We report on a wide array of systems: from disease-related proteins that undergo sulfurylation or phosphorylation through natural metallophores that selectively capture precious essential ions to synthetic selfassembly strategies, biocatalysts, and chelating agents against toxic metals. Regardless of their (bio)synthetic routes, all possess unique metal-binding properties that could not be effectively achieved by systems composed of canonical residues.

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Published

2021-06-30

How to Cite

[1]
L. Sauser, M. S. Shoshan, Chimia 2021, 75, 530, DOI: 10.2533/chimia.2021.530.