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Related Experiment Video

Updated: Nov 22, 2025

Quantitative SERS Detection of Uric Acid via Formation of Precise Plasmonic Nanojunctions within Aggregates of Gold Nanoparticles and Cucurbit[n]uril
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Protein recognition by cucurbit[6]uril: high affinity N-terminal complexation.

Kiefer O Ramberg1, Sylvain Engilberge1, Francesca Guagnini1

  • 1School of Chemistry, National University of Ireland Galway, University Road, Galway, H91 TK33, Ireland. peter.crowley@nuigalway.ie.

Organic & Biomolecular Chemistry
|January 6, 2021
PubMed
Summary

Cucurbit[n]urils (Qn) are macrocyclic receptors used in protein recognition. This study reveals cucurbit[6]uril (Q6) binds N-terminal methionine-lysine motifs in proteins, expanding Qn applications in molecular sensing.

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Area of Science:

  • Supramolecular Chemistry
  • Chemical Biology
  • Biophysical Chemistry

Background:

  • Cucurbit[n]urils (Qn) are macrocyclic hosts widely used for protein recognition, primarily targeting N-terminal aromatic residues with Q7 and Q8.
  • Cucurbit[6]uril (Q6) exhibits unique affinity for alkylamines, suggesting potential for recognizing lysine side chains, but its protein interactions are less explored.

Purpose of the Study:

  • To investigate the protein complexation capabilities of cucurbit[6]uril (Q6) using Nuclear Magnetic Resonance (NMR) spectroscopy.
  • To explore Q6's binding preferences beyond lysine residues and assess its potential for N-terminal recognition.

Main Methods:

  • Utilized NMR spectroscopy to study interactions between Q6 and four model proteins with varying properties.
  • Investigated Q6 binding to specific lysine residues (Lys) and dimethylated lysine residues.
  • Engineered N-terminal methionine-lysine motifs into model proteins to assess binding affinity.

Main Results:

  • Demonstrated Q6's ability to recognize specific lysine residues and N-terminal methionine-lysine motifs with high affinity (micromolar range).
  • Observed similar high-affinity binding when the Met-Lys motif was engineered into a different protein.
  • Provided evidence for cucurbit[8]uril (Q8) also binding to the N-terminal Met-Lys feature.

Conclusions:

  • Expands the known binding repertoire of cucurbiturils, particularly highlighting Q6's capacity for N-terminal protein recognition.
  • Establishes the N-terminal Met-Lys motif as a high-affinity binding site for Q6 and potentially Q8.
  • Enhances the utility of cucurbiturils as versatile tools for protein sensing and molecular recognition applications.