Design of a Selective Metal Ion Switch for Self-Assembly of Peptide-Based Fibrils

Dublin, Steven N.; Conticello, Vincent P.

doi:10.1021/ja0775016

Cited by 156Supramolecular Self-Assembly in MaterialsSupramolecular Chemistry and ComplexesChemical Synthesis and Analysis

Design of a Selective Metal Ion Switch for Self-Assembly of Peptide-Based Fibrils

Dublin, Steven N., Conticello, Vincent P.·2008·Journal of the American Chemical Society

DOI 10.1021/ja0775016

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Abstract

The self-assembling peptide TZ1H, a structural variant of the trimeric isoleucine zipper GCN4-pII, contains histidine residues at core d-positions of alternate heptads that define three trigonal coordination sites within the coiled-coil trimer. Circular dichroism spectropolarimetry indicated that peptide TZ1H undergoes a random coil to alpha-helical conformational change upon binding of 1 equiv of silver(I) ion, but not zinc(II), copper(II), or nickel(II) ions. Isothermal titration calorimetry provided evidence for a single binding-site model in which each peptide contributes one net silver(I) coordination site, in agreement with the proposed structural model. Transmission electron microscopy revealed that TZ1H self-assembles into long aspect ratio helical fibers in the presence of silver(I) ion. These results demonstrate that the rational design of selective metal ion binding sites within de novo designed peptides represents a promising approach to the controlled fabrication of nanoscale, self-assembled materials.

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Achieving the desired balance between multiple target coiled-coil states often requires several rounds of trial-and-error and a detailed understanding of the energetic factors that discriminate between alternative topologies and oligomerization states.
“While this has been accomplished in a number of cases,18−31 achieving the desired balance between multiple target coiled-coil states often requires several rounds of trial-and-error and a detailed understanding of the energetic factors that discriminate between alternative topologies and oligomerization states.”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [21]

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Authors: Dublin, S. N., & Conticello, V. P.
Affiliations: Emory University (US)
ORCID: Conticello, Vincent P.
Venue: Journal of the American Chemical Society
Publisher: American Chemical Society (ACS)
Published: 2007-12-08
Volume: 130
Issue: 1
Pages: 49-51
ISSN: 0002-7863 (ISSN-L)
1520-5126
DOI: 10.1021/ja0775016
OpenAlex: W1973386358
Cited by: 156
References: 27
Citations by year: 2026: 4 · 2025: 8 · 2024: 4 · 2023: 8 · 2022: 9 · 2021: 9 · 2020: 7 · 2019: 5 · 2018: 13 · 2017: 5 · 2016: 6 · 2015: 6 · 2014: 9 · 2013: 7 · 2012: 10
FWCI: 5.58
Type: journal article
Language: en
Open access: closed
Locations: Journal of the American Chemical Society (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Department of Energy
Division of Chemistry
Topics: Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
Physical Sciences › Chemistry › Organic Chemistry › Supramolecular Chemistry and Complexes
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
Keywords: peptide self-assembly, metal ion binding, silver(I) coordination, peptide fibrils, helical fibers, conformational change, de novo peptide design, peptide nanofibers
MeSH terms: Binding Sites, Metals, Microscopy, Electron, Peptides, Protein Conformation, Silver, Nanostructures

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Design of a Selective Metal Ion Switch for Self-Assembly of Peptide-Based Fibrils

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