TY - JOUR
T1 - Ion permeation by a folded multiblock amphiphilic oligomer achieved by hierarchical construction of self-assembled nanopores
AU - Muraoka, Takahiro
AU - Shima, Tatsuya
AU - Hamada, Tsutomu
AU - Morita, Masamune
AU - Takagi, Masahiro
AU - Tabata, Kazuhito V.
AU - Noji, Hiroyuki
AU - Kinbara, Kazushi
PY - 2012/12/5
Y1 - 2012/12/5
N2 - A multiblock amphiphilic molecule 1, 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 1 forms a 0.53 nm channel allowing for permeation of cations. Since neither 3, bearing flexible hydrophobic units and forming no stacked structures in the membrane, nor 2, a monomeric version of 1, is able to transport cations, the folded conformation of 1 in the membrane is likely essential for realizing its function. Thus, function and hierarchically formed higher-order structures of 1, is strongly correlated with each other like proteins and other biological macromolecules.
AB - A multiblock amphiphilic molecule 1, 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 1 forms a 0.53 nm channel allowing for permeation of cations. Since neither 3, bearing flexible hydrophobic units and forming no stacked structures in the membrane, nor 2, a monomeric version of 1, is able to transport cations, the folded conformation of 1 in the membrane is likely essential for realizing its function. Thus, function and hierarchically formed higher-order structures of 1, is strongly correlated with each other like proteins and other biological macromolecules.
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U2 - 10.1021/ja308342g
DO - 10.1021/ja308342g
M3 - Article
C2 - 23145887
AN - SCOPUS:84870688870
SN - 0002-7863
VL - 134
SP - 19788
EP - 19794
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 48
ER -