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Related Concept Videos

Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
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Related Experiment Video

Updated: May 21, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Intermolecular interactions in electron transfer through stretched helical peptides.

Daniel E López-Pérez1, Guillermo Revilla-López, Denis Jacquemin

  • 1Departament d'Enginyeria Química, ETSEIB, Universitat Politècnica de Catalunya, Av. Diagonal 647, 08028, Barcelona, Spain.

Physical Chemistry Chemical Physics : PCCP
|June 28, 2012
PubMed
Summary

This study reveals that the helical structure of peptides on gold surfaces is crucial for their electrical conductance. Peptides can stretch significantly before conductance ceases, with interactions stabilizing their helical form.

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Published on: February 5, 2020

Area of Science:

  • Molecular Biophysics
  • Nanotechnology
  • Surface Science

Background:

  • Self-assembled monolayers (SAMs) of helical peptides on gold surfaces are key components in molecular electronics.
  • Understanding peptide conductance under mechanical stress is vital for designing novel electronic devices.

Purpose of the Study:

  • To investigate the conductance behavior of helical peptides organized as a self-assembled monolayer on gold.
  • To elucidate the role of helical conformation and intermolecular interactions in peptide conductance.
  • To determine the critical elongation of peptides before conductance loss.

Main Methods:

  • Experimental techniques: Scanning tunnelling microscopy (STM) and current sensing atomic force microscopy (CS-AFM).
  • Computational methods: Molecular dynamics (MD) simulations and quantum mechanical (QM) calculations.
  • Fabrication of peptide monolayers on gold surfaces at varying densities.

Main Results:

  • Helical peptide conformation significantly influences conductance.
  • Peptides exhibit substantial elongation (1.22 ± 0.47 nm) before conductance drops to zero.
  • MD simulations confirmed helical stability in solvated and desolvated environments due to peptide-peptide interactions.
  • Simulations identified ionic ladders, suggesting peptide-mediated electron transfer via hopping.
  • QM calculations analyzed electronic structure changes during mechanical deformation.

Conclusions:

  • The helical conformation is essential for peptide conductance on gold surfaces.
  • Intermolecular peptide interactions stabilize the helical structure, even in desolvated conditions.
  • Peptide-mediated electron transfer likely occurs through a hopping mechanism.
  • The study provides insights into the mechanical and electronic properties of peptide-based nanostructures.