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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Related Experiment Video

Updated: Apr 5, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Electron Transfer Mechanism in Helical Peptides.

Himadri Shekhar Mandal1, Heinz-Bernhard Kraatz1

  • 1Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, SK S7N 5C9, Canada.

The Journal of Physical Chemistry Letters
|August 20, 2015
PubMed
Summary

Electron transfer in ferrocene-labeled peptides showed weak distance dependence. This is attributed to a dynamic tunneling mechanism involving helical conformation changes in self-assembled monolayers.

Keywords:
helixpeptide

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Area of Science:

  • Electrochemistry
  • Biophysical Chemistry
  • Materials Science

Background:

  • Ferrocene-labeled peptides are used to study electron transfer.
  • Self-assembled monolayers (SAMs) on gold electrodes provide a platform for electrochemical studies.
  • Helical peptide structure can influence electron transfer rates.

Purpose of the Study:

  • To investigate the distance dependence of electron transfer (ET) in ferrocene-labeled helical peptides.
  • To elucidate the mechanism governing ET in self-assembled monolayers (SAMs).
  • To explore the role of peptide conformation in electron transfer.

Main Methods:

  • Electrochemical studies using cyclic voltammetry.
  • Formation of self-assembled monolayers (SAMs) of peptides on gold electrodes.
  • Varying peptide length to probe distance effects on electron transfer.

Main Results:

  • Electron transfer rates exhibited very weak distance dependence.
  • The observed ET behavior suggests a dynamically controlled tunneling mechanism.
  • A slow equilibrium between alpha- and 310-helical conformations was identified.

Conclusions:

  • The dynamic equilibrium between helical conformers influences electron transfer.
  • The rate of formation of the more conductive 310 conformer is linked to observed ET rates.
  • This work provides insights into electron transfer mechanisms in biomolecular systems.