ZiCo: A Peptide Designed to Switch Folded State upon Binding Zinc
Abstract
We describe a novel approach to the design of a metal-triggered conformational switch. Specifically, two distinct protein-folding motifs were merged into one polypeptide sequence. The target structures were an alpha-helical coiled-coil trimer and zinc-bound monomer. Solution-phase spectroscopic, sedimentation, and binding studies confirmed the key aspects of the design. Both forms of the peptide were cooperatively folded, and the switch between them was reversible. This design process potentially presents a novel route to peptide-based biosensors.
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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 [18]
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Dishman, A. F., & Volkman, B. F. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102380 · Cited by 36 · see citing works
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- Authors
- Cerasoli, E., Sharpe, B. K., & Woolfson, D. N.
- Affiliations
- University of Sussex (GB)
- ORCID
- Woolfson, Derek N.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-10-08
- Volume
- 127
- Issue
- 43
- Pages
- 15008-15009
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1980254610
- Cited by
- 104
- References
- 0
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 1 · 2023: 2 · 2022: 1 · 2021: 5 · 2020: 3 · 2019: 5 · 2018: 2 · 2017: 2 · 2016: 6 · 2015: 3 · 2014: 1 · 2013: 4 · 2012: 11
- FWCI
- 3.36
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of the American Chemical Society (publishedVersion)
- PubMed (publishedVersion)
- Bristol Research (University of Bristol) (publishedVersion)
- Explore Bristol Research (submittedVersion)
- Funders
- Biotechnology and Biological Sciences Research Council (B17958/2)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- zinc binding, peptide design, protein folding, cooperative folding, peptide-based biosensors, metalloproteins
- MeSH terms
- Binding Sites, Chlorides, Circular Dichroism, Edetic Acid, Peptides, Temperature, Zinc, Protein Structure, Secondary, Protein Folding, Spectroscopy, Fourier Transform Infrared, Zinc Compounds
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