ArticleChemical science2019
Selective coordination of three transition metal ions within a coiled-coil peptide scaffold.
Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Design of a site selective heterochromic bimetallic lanthanide coiled coil with nanometre-scale control.Chemical science · 2026Article
- Metal Ion-Specific Modulation of Network Connectivity and Defects in Poly(ethylene glycol)-Peptide Conjugate Assemblies and Hydrogels.Chemistry of materials : a publication of the American Chemical Society · 2026Article
- Sequence Prediction, Structural Modelling and the Challenges of Plasticity in Coiled Coils.Sub-cellular biochemistry · 2026Review
- A De Novo Designed Metalloprotein Displays Variable Thermal Stability and Binding Stoichiometry with Transition Metal Ions.Chembiochem : a European journal of chemical biology · 2025Article
- Design of the elusive proteinaceous oxygen donor copper site suggests a promising future for copper for MRI contrast agents.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Azobenzene-Based Amino Acids for the Photocontrol of Coiled-Coil Peptides.Bioconjugate chemistry · 2023Article
- An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnChembiochem : a European journal of chemical biology · 2023Article
- A Structural Analysis of Proteinaceous Nanotube Cavities and Their Applications in Nanotechnology.Nanomaterials (Basel, Switzerland) · 2022Review
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Metal ion-regulated assembly of designed modular protein cages.Science advances · 2022Article
- Phase separation and zinc-induced transition modulate synaptic distribution and association of autism-linked CTTNBP2 and SHANK3.Nature communications · 2022Article
- De novo metalloprotein design.Nature reviews. Chemistry · 2022Article
- Coiled coils 9-to-5: rationalChemical science · 2021Article
- Conformational control in a photoswitchable coiled coil.Chemical communications (Cambridge, England) · 2021Article
- Self-assembly and regulation of protein cages from pre-organised coiled-coil modules.Nature communications · 2021Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Designing peptides that fold and assemble in response to metal ions tests our understanding of how peptide folding and metal binding influence one another. Here, histidine residues are introduced into the hydrophobic core of a coiled-coil trimer, generating a peptide that self-assembles upon the addition of metal ions. HisAD, the resulting peptide, is unstructured in the absence of metal and folds selectively to form an α-helical construct upon complexation with Cu(ii) and Ni(ii) but not Co(ii) or Zn(ii). The structure, and metal-binding ability, of HisAD is probed using a combination of circular dichroism (CD) spectroscopy, analytical ultracentrifugation (AUC), nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography. These show the peptide is trimeric and binds to both Cu(ii) and Ni(ii) in a 1 : 1 ratio with the histidine residues involved in the metal coordination, as designed. The X-ray crystal structure of the HisAD-Cu(ii) complex reveals the trimeric HisAD peptide coordinates three Cu(ii) ions; this is the first example of such a structure. Additionally, HisAD demonstrates an unprecedented discrimination between transition metal ions, the basis of which is likely to be related to the stability of the peptide-metal complexes formed.
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Registered trials
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