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Catechols as Membrane Anion Transporters
Author(s) -
Sofya Kostina Berezin,
Jeffery T. Davis
Publication year - 2009
Publication title -
journal of the american chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.115
H-Index - 612
eISSN - 1520-5126
pISSN - 0002-7863
DOI - 10.1021/ja809733c
Subject(s) - chemistry , catechol , amphiphile , selectivity , membrane , transporter , transmembrane protein , membrane transport , liposome , combinatorial chemistry , ion transporter , biophysics , biochemistry , organic chemistry , polymer , receptor , copolymer , catalysis , gene , biology
We report that an amphiphilic bis-catechol (3) functions as a transmembrane anion transporter. Activity depends on the catechol's substitution and amphiphilicity. We also describe a liposomal assay that allows one to readily measure anion transport selectivity. This assay reveals that anion transport selectivity for this amphiphilic bis-catechol follows a Hofmeister sequence wherein anions that are easier to dehydrate are made more permeable to the membrane by 3.

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