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Visualizing cyclic peptide hydration at the single-molecule level.

ABSTRACT: The role of water molecules in the selective transport of potassium ions across cell membranes is important. Experimental investigations of valinomycin-water interactions remain huge challenge due to the poor solubility of valinomycin in water. Herein, we removed this experimental obstacle by introducing gaseous water and valinomycin onto a Cu(111) surface to investigate the hydration of valinomycin. By combining scanning tunneling microscopy (STM) with density functional theory (DFT) calculations, we revealed that water could affect the adsorption structure of valinomycin. Hydrogen bond interactions occurred primarily at the carbonyl oxygen of valinomycin and resulted in the formation of valinomycin hydrates. The single-molecule perspective revealed in our investigation could provide new insight into the role of water on the conformation transition of valinomycin, which might provide a new molecular basis for the ion transport mechanism at the water/membrane interface.

SUBMITTER: Chen Y

PROVIDER: S-EPMC3746206 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Visualizing cyclic peptide hydration at the single-molecule level.

Chen Yumin Y Deng Ke K Qiu Xiaohui X Wang Chen C

Scientific reports 20130101

The role of water molecules in the selective transport of potassium ions across cell membranes is important. Experimental investigations of valinomycin-water interactions remain huge challenge due to the poor solubility of valinomycin in water. Herein, we removed this experimental obstacle by introducing gaseous water and valinomycin onto a Cu(111) surface to investigate the hydration of valinomycin. By combining scanning tunneling microscopy (STM) with density functional theory (DFT) calculatio ...[more]

PMID: 23955234

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