Sequence-defined oligomeric molecules with discrete folding propensities, termed foldamers, are a versatile source of agents with tailored structure and function. An inspiration for the development of the foldamer paradigm are natural biomacromolecules, the sequence-encoded folding of which is the basis of life. Metal ions and clusters are common features in proteins, where the role of metal varies from supporting structure to enabling function. The ubiquity of metals in natural systems suggests promise for metals in the context of folded artificial backbones. In this Minireview, we highlight efforts to realize this potential through a survey of published work on the design, synthesis, and characterization of metal-binding foldamers.
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http://dx.doi.org/10.1002/cplu.202000730 | DOI Listing |
Chem Commun (Camb)
January 2025
Department of Chemistry, Indian Institute of Science Education and Research (IISER), Pune, Dr Homi Bhabha Road, Pune-411008, India.
A superhelix is a three-dimensional arrangement of a helix in which the helix is coiled around a common axis. Here, we are reporting a short 12-helix of α,γ-hybrid peptides terminated by metal binding ligands, self-assembled into a right-handed superhelix around a common axis in the presence of Cd(II) ions. Furthermore, these superhelices are assembled into hierarchical superhelical β-sheet-type structural motifs in single crystals.
View Article and Find Full Text PDFInt J Mol Sci
November 2022
Department of Chemical Biology, Faculty of Biotechnology, University of Wrocław, Joliot-Curie 14a, 50-383 Wrocław, Poland.
Classical zinc fingers domains (ZFs) bind Zn(II) ion by a pair of cysteine and histidine residues to adopt a characteristic and stable ββα fold containing a small hydrophobic core. As a component of transcription factors, they recognize specific DNA sequences to transcript particular genes. The loss of Zn(II) disrupts the unique structure and function of the whole protein.
View Article and Find Full Text PDFChempluschem
January 2021
Department of Chemistry, University of Pittsburgh, Pittsburgh, PA, 15260, USA.
Sequence-defined oligomeric molecules with discrete folding propensities, termed foldamers, are a versatile source of agents with tailored structure and function. An inspiration for the development of the foldamer paradigm are natural biomacromolecules, the sequence-encoded folding of which is the basis of life. Metal ions and clusters are common features in proteins, where the role of metal varies from supporting structure to enabling function.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
June 2018
Schulich Faculty of Chemistry, Technion-Israel Institute of Technology, Technion City, Haifa, 3200008, Israel.
Metal-ligand coordination is a key interaction in the self-assembly of both biopolymers and synthetic oligomers. Although the binding of metal ions to synthetic proteins and peptides is known to yield high-order structures, the self-assembly of peptidomimetic molecules upon metal binding is still challenging. Herein we explore the self-assembly of three peptoid trimers bearing a bipyridine ligand at their C-terminus, a benzyl group at their N-terminus, and a polar group (N-ethyl-R) in the middle position (R=OH, OCH , or NH ) upon Cu coordination.
View Article and Find Full Text PDFChem Commun (Camb)
March 2018
Department of Molecular Design and Engineering, Graduate School of Engineering, Nagoya University, Chikusa-ku, Nagoya 464-8603, Japan.
A helical foldamer possessing conformationally switchable metal-binding linkers underwent supramolecular polymerization to form a helical nanofiber. A reversible helix-to-helix transition of the helical nanofiber took place upon cooperative binding and release of Ag(i) ions via a metal-coordination-driven W-to-U-shape conformational change of the linkers in a positive allosteric manner.
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