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Cited by 25Protein Structure and DynamicsChemical Synthesis and AnalysisBiochemical and Structural Characterization

Coiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection

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Mueller, Carolin, Grossmann, Tom N.·2018·Angewandte Chemie International Edition
DOI 10.1002/anie.201811515PMC PMC6391972
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Abstract

The understanding of protein folding and assembly is of central importance for the design of proteins and enzymes with novel or improved functions. Minimalistic model systems, such as coiled-coils, provide an excellent platform to improve this understanding and to construct novel molecular devices. Along those lines, we designed a conformational switch that is composed of two coiled-coil forming peptides and a central binding epitope. In the absence of a binding partner, this switch adopts a hairpin-like conformation that opens upon receptor binding. Variation of the coiled-coil length modulates the strength of the intramolecular constraint. The two conformational states of this switch have been linked with characteristic fluorescent properties, which enables the detection of the receptor in real-time.

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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 [27]

    The paper’s Abstract (page unavailable) describes a coiled-coil switch with two conformational states and shows that changing coiled-coil length tunes its stability. It therefore supports the preceding, citation-attached point that such a switch has been achieved. It does not say that achieving the desired balance often requires several rounds of trial-and-error or detailed knowledge of energetic discrimination between alternative topologies and oligomerization states. (LLM, conf=0.82)

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Authors
Mueller, C., & Grossmann, T. N.
Affiliations
Vrije Universiteit Amsterdam (NL)
Corresponding author
Grossmann, Tom N.
ORCID
Grossmann, Tom N.
Venue
Angewandte Chemie International Edition
Publisher
Wiley
Published
2018-11-28
Volume
57
Issue
52
Pages
17079-17083
ISSN
  • 1433-7851 (ISSN-L)
  • 1521-3773
DOI
10.1002/anie.201811515
PMC
PMC6391972
OpenAlex
W2899615021
Cited by
25
References
55
Citations by year
2025: 5 · 2024: 6 · 2023: 2 · 2022: 3 · 2021: 4 · 2020: 4 · 2019: 1
FWCI
0.80
Type
journal article
Language
en
Open access
Licence
Locations
  • Angewandte Chemie International Edition (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • VU Research Portal (publishedVersion, other-oa)
  • Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
Funders
H2020 European Research Council (678623)
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
coiled-coil peptides, conformational switching, protein detection, receptor binding, hairpin conformation, fluorescent biosensor, protein folding, protein assembly, molecular devices
MeSH terms
Fluorescence, Models, Molecular, Peptides, Protein Conformation, Proteins, Protein Folding

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