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Energy to Drive Translocation

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Characterization of Intra-Cartilage Transport Properties of Cationic Peptide Carriers
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Published on: August 10, 2020

Distal charge transport in peptides.

Edward W Schlag1, Sheh-Yi Sheu, Dah-Yen Yang

  • 1Institut für Physikalische und Theoretische Chemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany. schlag@mytum.de

Angewandte Chemie (International Ed. in English)
|March 21, 2007
PubMed
Summary

This study introduces an atomistic model for charge and reactivity transport in peptides. It reveals highly efficient transport within peptides but low efficiency in water, suggesting ultrafast biological processes.

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Last Updated: Jul 16, 2026

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Area of Science:

  • Biochemistry
  • Chemical Kinetics
  • Molecular Biophysics

Background:

  • Biological systems exhibit charge and reactivity transport over long distances, a phenomenon not fully explained by traditional chemical kinetics.
  • Existing models often fail to capture these extreme distal processes in biological molecules.

Purpose of the Study:

  • To present an atomistic model for distal information transport, specifically tailored for peptides.
  • To investigate the mechanisms and efficiency of charge and reactivity transport in peptides using a novel kinetic model.

Main Methods:

  • Consideration of an atomistic model for distal transport of information in peptides.
  • Application of a two-step bifunctional kinetic model to describe chemical reactivity.
  • Analysis of peptide motional properties in the subpicosecond regime.

Main Results:

  • The bifunctional model demonstrates highly efficient transport of charge and reactivity within an isolated peptide over substantial distances.
  • A significantly lower efficiency of charge and reactivity transport was observed in a water environment.
  • The model predicts ultrafast transport capabilities over considerable molecular distances in a peptide setting.

Conclusions:

  • The proposed model elucidates ultrafast charge and reactivity transport in peptides, crucial for biological functions.
  • This mechanism highlights the potential for numerous active domains within proteins to facilitate long-range biological processes.
  • The findings challenge traditional kinetic models by accounting for distal effects and rapid peptide dynamics.