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Ligand‐Induced Extramembrane Conformation Switch Controlling Alamethicin Assembly and the Channel Current
Author(s) -
Futaki Shiroh,
Asami Koji
Publication year - 2007
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200790112
Subject(s) - alamethicin , chemistry , leucine zipper , ion channel , biophysics , gating , membrane , ligand (biochemistry) , current (fluid) , receptor , biochemistry , peptide sequence , biology , gene , engineering , electrical engineering
Abstract In this review, we describe our approach to creating artificial receptor‐channel proteins or sensor systems, using an extramembrane segment conformationally switchable by external stimuli. Alamethicin is known to self‐assemble in membranes to form ion channels with various open states. Employment of an α ‐helical leucine‐zipper segment resulted in the effective modulation of the association states of alamethicin to produce a single predominant channel‐open state. A decrease in the helical content of the extramembrane segments was found to induce a channel‐current increase. Therefore, conformational changes in the extramembrane segments induced by the interaction with ligands can be reflected in the current levels.