Ion-Pairing Mechanism for the Valinomycin-Mediated Transport of Potassium Ions across Phospholipid Bilayers

The role of the anion on the ionophore properties of valinomycin was studied in a model floating bilayer lipid membrane (fBLM) using supporting electrolytes containing K+ with four different counter anion species (ClO4-, H2PO4-, Cl-, and F-). The electrochemical impedance spectra indicate that the m...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 37(2021), 31 vom: 10. Aug., Seite 9613-9621
1. Verfasser: Su, ZhangFei (VerfasserIn)
Weitere Verfasser: Leitch, J Jay, Sek, Slawomir, Lipkowski, Jacek
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Cations Ionophores Lipid Bilayers Phospholipids Valinomycin 2001-95-8 Potassium RWP5GA015D
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520 |a The role of the anion on the ionophore properties of valinomycin was studied in a model floating bilayer lipid membrane (fBLM) using supporting electrolytes containing K+ with four different counter anion species (ClO4-, H2PO4-, Cl-, and F-). The electrochemical impedance spectra indicate that the membrane resistance of the bilayer decreases with the decrease of Gibbs free energy of anion solvation. The IR spectra demonstrate that valinomycin does not readily bind to K+ in the KH2PO4, KCl, and KF electrolyte solutions, but in the presence of KClO4, valinomycin readily binds to K+, forming a valinomycin-K+ complex. The results in the present paper reveal the role of the counter anion on the transport of cations by valinomycin across the lipid bilayer. The valinomycin-cation complex creates an ion pair with the anion, and this ion pair can enter the hydrophobic region of the bilayer transporting the cation across the membrane. Anions with low solvation energies facilitate the formation of the ion pair improving the ion conductivity of valinomycin-incorporated bilayers. This paper sheds new light on the transport mechanism of valinomycin ionophores and provides new information about the bioactivity of this molecule 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Ionophores  |2 NLM 
650 7 |a Lipid Bilayers  |2 NLM 
650 7 |a Phospholipids  |2 NLM 
650 7 |a Valinomycin  |2 NLM 
650 7 |a 2001-95-8  |2 NLM 
650 7 |a Potassium  |2 NLM 
650 7 |a RWP5GA015D  |2 NLM 
700 1 |a Leitch, J Jay  |e verfasserin  |4 aut 
700 1 |a Sek, Slawomir  |e verfasserin  |4 aut 
700 1 |a Lipkowski, Jacek  |e verfasserin  |4 aut 
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