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Updated: May 8, 2026

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Visualizing cyclic peptide hydration at the single-molecule level.

Yumin Chen1, Ke Deng, Xiaohui Qiu

  • 1National Center for Nanoscience and Technology, China, Beijing 100190, PR China.

Scientific Reports
|August 20, 2013
PubMed
Summary
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Investigating valinomycin hydration, this study used scanning tunneling microscopy and density functional theory. Water molecules form hydrogen bonds with valinomycin, influencing its structure and potentially ion transport mechanisms.

Area of Science:

  • Biophysical Chemistry
  • Surface Science
  • Computational Chemistry

Background:

  • Water molecules play a crucial role in selective ion transport across cell membranes.
  • Investigating valinomycin-water interactions is experimentally challenging due to valinomycin's poor water solubility.

Purpose of the Study:

  • To overcome experimental limitations in studying valinomycin hydration.
  • To elucidate the molecular-level interactions between water and valinomycin.

Main Methods:

  • Utilized scanning tunneling microscopy (STM) to observe valinomycin on a Cu(111) surface.
  • Employed density functional theory (DFT) calculations to analyze valinomycin-water interactions.
  • Introduced gaseous water and valinomycin onto a metal surface to enable study.

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Related Experiment Videos

Last Updated: May 8, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Main Results:

  • Water molecules were found to affect the adsorption structure of valinomycin.
  • Hydrogen bonding predominantly occurred at the carbonyl oxygen of valinomycin.
  • Formation of valinomycin hydrates was observed, providing a single-molecule perspective.

Conclusions:

  • The study provides new insights into how water influences valinomycin conformation.
  • Findings offer a potential molecular basis for understanding ion transport at water/membrane interfaces.
  • This research addresses the challenge of studying poorly soluble compounds in aqueous environments.