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Enhancing Metal-binding with Noncanonical Coordinating Amino Acids


Sauser, Luca; Shoshan, Michal S (2021). Enhancing Metal-binding with Noncanonical Coordinating Amino Acids. Chimia, 75(6):530.

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.

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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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Scopus Subject Areas:Physical Sciences > General Chemistry
Uncontrolled Keywords:General Medicine, General Chemistry
Language:English
Date:30 June 2021
Deposited On:08 Feb 2022 15:22
Last Modified:26 Apr 2024 01:41
Publisher:Swiss Chemical Society
ISSN:0009-4293
Additional Information:Copyright ©Swiss Chemical Society: CHIMIA, 75(6):530, 2021
OA Status:Gold
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.2533/chimia.2021.530
PubMed ID:34233819
Project Information:
  • : FunderSNSF
  • : Grant IDPZ00P2_179818
  • : Project TitleSelective Heavy Metal Detoxification by Short Peptides: A New Approach for Chelation Therapy
  • : FunderUZH Forschungskredit
  • : Grant IDK-73521-11-01
  • : Project Title
  • Content: Published Version
  • Licence: Creative Commons: Attribution 4.0 International (CC BY 4.0)