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Related Concept Videos

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Related Experiment Video

Updated: Jan 20, 2026

Visualization of Surface-tethered Large DNA Molecules with a Fluorescent Protein DNA Binding Peptide
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Conductance Switching in Single-Peptide Molecules through Interferer Binding.

Li-Wen Huang1,2, Yen-Hsun Su2, Chao-Cheng Kaun1,3

  • 1Research Center for Applied Sciences, Academia Sinica, Taipei 11529, Taiwan, Republic of China.

ACS Omega
|August 29, 2019
PubMed
Summary
This summary is machine-generated.

Peptide single-molecule junctions can detect harmful copper ions (Cu2+) and bisphenol A (BPA). The cysteamine-Gly-Gly-Cys junction shows superior sensing capabilities for these molecules compared to Cys-Gly-Cys.

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Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
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Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
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Area of Science:

  • Molecular electronics
  • Biosensing
  • Computational chemistry

Background:

  • Detecting bioprocess-interfering molecules like copper ions (Cu2+) and bisphenol A (BPA) is crucial for healthcare.
  • Peptide single-molecule junctions offer a promising platform for efficient sensing of these targets.

Purpose of the Study:

  • To investigate the conductance of Cys-Gly-Cys and cysteamine-Gly-Gly-Cys peptide junctions.
  • To determine the effect of Cu2+ and BPA binding on the conductance of these peptide junctions.

Main Methods:

  • First-principles calculations were employed to simulate and analyze the electronic conductance of peptide junctions.
  • The study compared calculated conductance values with existing experimental data for Cu2+ binding.

Main Results:

  • Calculated conductance for peptides and Cu2+ complexes aligned well with experimental data.
  • The binding of BPA to peptides was predicted, revealing distinct conductance changes.
  • Cu2+ binding induced conductance switching via structural deformation, while BPA binding created new conduction channels.

Conclusions:

  • The cysteamine-Gly-Gly-Cys peptide junction demonstrates enhanced recognition capabilities for both Cu2+ and BPA compared to the Cys-Gly-Cys junction.
  • These findings highlight the potential of tailored peptide sequences in molecular electronics for targeted analyte detection.