title: Biomimetic Transmembrane Channels with High Stability and Transporting Efficiency from Helically Folded Macromolecules.
abstract: Membrane channels span the cellular lipid bilayers to transport ions and molecules into cells with sophisticated properties including high efficiency and selectivity. It is of particular biological importance in developing biomimetic transmembrane channels with unique functions by means of chemically synthetic strategies. An artificial unimolecular transmembrane channel using pore-containing helical macromolecules is reported. The self-folding, shape-persistent, pore-containing helical macromolecules are able to span the lipid bilayer, and thus result in extraordinary channel stability and high transporting efficiency for protons and cations. The lifetime of this artificial unimolecular channel in the lipid bilayer membrane is impressively long, rivaling those of natural protein channels. Natural channel mimics designed by helically folded polymeric scaffolds will display robust and versatile transport-related properties at single-molecule level.
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun, 130012, P.R. China.
authors.forename: Chao
authors.initials: C
authors.lastname: Lang
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun, 130012, P.R. China.
authors.forename: Wenfang
authors.initials: W
authors.lastname: Li
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun, 130012, P.R. China. zdong@jlu.edu.cn.
authors.forename: Zeyuan
authors.initials: Z
authors.lastname: Dong
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun, 130012, P.R. China.
authors.forename: Xin
authors.initials: X
authors.lastname: Zhang
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun, 130012, P.R. China.
authors.forename: Feihu
authors.initials: F
authors.lastname: Yang
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun, 130012, P.R. China.
authors.forename: Bing
authors.initials: B
authors.lastname: Yang
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun, 130012, P.R. China.
authors.forename: Xiaoli
authors.initials: X
authors.lastname: Deng
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun, 130012, P.R. China.
authors.forename: Chenyang
authors.initials: C
authors.lastname: Zhang
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun, 130012, P.R. China.
authors.forename: Jiayun
authors.initials: J
authors.lastname: Xu
authors.affiliation: State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Street, Changchun, 130012, P.R. China. junqiuliu@jlu.edu.cn.
authors.forename: Junqiu
authors.initials: J
authors.lastname: Liu
keywords: cation transport; helical folding; helical macromolecules; pore structure; transmembrane channels