Muraoka, Takahiro Shima, Tatsuya Hamada, Tsutomu Morita, Masamune Takagi, Masahiro Tabata, Kazuhito V. Noji, Hiroyuki Kinbara, Kazushi Ion Permeation by a Folded Multiblock Amphiphilic Oligomer Achieved by Hierarchical Construction of Self-Assembled Nanopores A multiblock amphiphilic molecule <b>1</b>, with a tetrameric alternating sequence of hydrophilic and hydrophobic units, adopts a folded structure in a liposomal membrane like a multipass transmembrane protein, and is able to transport alkali metal cations through the membrane. Hill’s analysis and conductance measurements, analyzed by the Hille equation, revealed that the tetrameric assembly of <b>1</b> forms a 0.53 nm channel allowing for permeation of cations. Since neither <b>3</b>, bearing flexible hydrophobic units and forming no stacked structures in the membrane, nor <b>2</b>, a monomeric version of <b>1</b>, is able to transport cations, the folded conformation of <b>1</b> in the membrane is likely essential for realizing its function. Thus, function and hierarchically formed higher-order structures of <b>1</b>, is strongly correlated with each other like proteins and other biological macromolecules. Hille equation;1 forms;Hierarchical Construction;0.53 nm channel;ion Permeation;transport cations;liposomal membrane;function;Folded Multiblock Amphiphilic Oligomer Achieved;transport alkali metal cations;monomeric version;tetrameric assembly;multipass transmembrane protein;conductance measurements 2012-12-05
    https://acs.figshare.com/articles/media/Ion_Permeation_by_a_Folded_Multiblock_Amphiphilic_Oligomer_Achieved_by_Hierarchical_Construction_of_Self_Assembled_Nanopores/2463973
10.1021/ja308342g.s002