Synchronization of opening and closing of two gramicidin A channels pulled together by a linker: possible relevance to channel clustering

Abstract

The linear 15-mer peptide gramicidin A (gA) produced by Bacillus brevis is known to form the simplest natural ion channel in lipid membranes representing a head-to-head transmembrane dimer. Its incorporation...

Cholesterol-induced deformation of the gramicidin-A channel inhibiting potassium ion binding and transport

“…[24] Furthermore, once two gA channels are connected by a linker, their lifetime will be significantly increased. [25][26][27] Cholesterol (CHOL), as a major lipid component of plasma membranes of mammalian cells, exhibits significant impact on the conformation and activity of a variety of ion channels. [28][29][30][31][32][33][34] For gA, some experimental studies have shown that gA channel inactivation occurs in CHOLcontaining erythrocyte membranes and the rate of channel inactivation is strongly dependent on the phospholipid-to-CHOL molar ratio in the membrane.…”