How Valinomycin lonophores Enter and-Transport K+ across Model Lipid Bilayer Membranes

被引:43
|
作者
Su, ZhangFei [1 ]
Ran, XueQin [2 ,3 ]
Leitch, J. Jay [1 ]
Schwan, Adrian L. [1 ]
Faragher, Robert [1 ]
Lipkowski, Jacek [1 ]
机构
[1] Univ Guelph, Dept Chem, Guelph, ON N1G 2W1, Canada
[2] Nanjing Tech Univ NanjingTech, Jiangsu Natl Synerget Innovat Ctr Adv Mat SICAM, KLOFE, 30 South Puzhu Rd, Nanjing 211816, Peoples R China
[3] Nanjing Tech Univ NanjingTech, Jiangsu Natl Synerget Innovat Ctr Adv Mat SICAM, IAM, 30 South Puzhu Rd, Nanjing 211816, Peoples R China
基金
加拿大自然科学与工程研究理事会;
关键词
INFRARED-ABSORPTION SPECTROSCOPY; ION-TRANSPORT; CRYSTAL-STRUCTURE; ORGANIC-SOLVENTS; PM-IRRAS; GRAMICIDIN; ELECTROCHEMISTRY; PEPTIDES; BINDING; NMR;
D O I
10.1021/acs.langmuir.9b03064
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Valinomycin, a cyclic peptide, was incorporated into a biomimetic lipid membrane tethered to' the surface of a gold (111) electrode. Electrochemical impedance spectroscopy was used to study the ionophore properties of the peptide, and polarization modulation infrared reflection absorption spectroscopy was employed to determine the conformation and orientation of valinomycin in the membrane. The combination of these two techniques provided unique information about the ionophore mechanism where valinomycin transports ions across the membrane by creating a complex with potassium ions and forming an ion pair with a counter anion. The ion pair resides within the hydrophobic fragment of the membrane and adopts a small angle of similar to 22 degrees with respect to the surface normal. This novel study provides new insights explaining the valinomycin ion transport mechanism in model biological membranes.
引用
收藏
页码:16935 / 16943
页数:9
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