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Peer-reviewedCC BYRSC chemical biology

Solution structure of a peptide-conjugated aggregation-induced-emission (AIE) fluorophore bound to a protein

  • Daniel Seifert1
  • Matthias Hayduk2
  • Torsten Herrmann3
  • David Podlesainski4
  • Jill Rohde1
  • Jürgen Linders5
  • Markus Kaiser4
  • Peter Bayer1
  • Jens Voskuhl2
  • Christine Beuck1
5 affiliations
  1. 1aStructural and Medicinal Biochemistry, University of Duisburg-Essen, Essen, Germany.
  2. 2bFaculty of Chemistry (Organic Chemistry), University of Duisburg-Essen, Essen, Germany.
  3. 3cInstitute of Structural Biology, Grenoble Alpes University, Grenoble, France.
  4. 4dChemical Biology, University of Duisburg-Essen, Essen, Germany.
  5. 5ePhysical Chemistry, University of Duisburg-Essen, Essen, Germany.
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Abstract

Here, we present a class of peptide-conjugated fluorophores based on aromatic thioethers with aggregation-induced emission (AIE) properties for specific recognition of small proteins and also the first solution NMR structure of an AIE ligand specifically bound to a protein. Binding of the hPin1-WW domain as a model protein resulted in a significant fluorescence increase, making these AIE-peptide fluorophores suitable as direct readout probes for specific protein interactions. Autofluorescence and protein-binding properties were elucidated as a function of peptide length and fluorophore concentration. While an AIE fluorophore with two conjugated peptides shows an enhanced fluorescence increase upon protein binding, a one-armed derivative enabled us to solve the structures of the free AIE-peptide and its complex. In the absence of a protein, the AIE-peptide conjugate shows a curled-up conformation that still allows rotation of the aromatic rings of the AIE-core, thus resulting in low auto-fluorescence. In contrast, the AIE-peptide unfurls upon binding, allowing the hPin1-WW domain to interact with its peptide recognition sequence. The aromatic rings of the AIE-core form additional contacts with the protein surface, which restricts their motions and thus results in the observed fluorescence increase.

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Cite

BibTeXRIS
BibTeX
@article{seifert2026solution,
  title = {{Solution structure of a peptide-conjugated aggregation-induced-emission (AIE) fluorophore bound to a protein}},
  author = {Daniel Seifert and Matthias Hayduk and Torsten Herrmann and David Podlesainski and Jill Rohde and Jürgen Linders and Markus Kaiser and Peter Bayer and Jens Voskuhl and Christine Beuck},
  journal = {RSC chemical biology},
  year = {2026},
  month = oct,
  doi = {10.1039/d6cb00109b},
  url = {https://europepmc.org/article/PMC/PMC13670144},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Solution structure of a peptide-conjugated aggregation-induced-emission (AIE) fluorophore bound to a protein
AU  - Daniel Seifert
AU  - Matthias Hayduk
AU  - Torsten Herrmann
AU  - David Podlesainski
AU  - Jill Rohde
AU  - Jürgen Linders
AU  - Markus Kaiser
AU  - Peter Bayer
AU  - Jens Voskuhl
AU  - Christine Beuck
PY  - 2026
DA  - 2026/10/01
JO  - RSC chemical biology
DO  - 10.1039/d6cb00109b
UR  - https://europepmc.org/article/PMC/PMC13670144
AB  - Here, we present a class of peptide-conjugated fluorophores based on aromatic thioethers with aggregation-induced emission (AIE) properties for specific recognition of small proteins and also the first solution NMR structure of an AIE ligand specifically bound to a protein. Binding of the hPin1-WW domain as a model protein resulted in a significant fluorescence increase, making these AIE-peptide fluorophores suitable as direct readout probes for specific protein interactions. Autofluorescence and protein-binding properties were elucidated as a function of peptide length and fluorophore concentration. While an AIE fluorophore with two conjugated peptides shows an enhanced fluorescence increase upon protein binding, a one-armed derivative enabled us to solve the structures of the free AIE-peptide and its complex. In the absence of a protein, the AIE-peptide conjugate shows a curled-up conformation that still allows rotation of the aromatic rings of the AIE-core, thus resulting in low auto-fluorescence. In contrast, the AIE-peptide unfurls upon binding, allowing the hPin1-WW domain to interact with its peptide recognition sequence. The aromatic rings of the AIE-core form additional contacts with the protein surface, which restricts their motions and thus results in the observed fluorescence increase.
SN  - 2633-0679
ER  -