Abstract
Abstract Gramicidin A (gA) is a kind of antibiotic peptide produced by Bacillus brevis and it can dimerize across lipid bilayers to form a monovalent cation channel. In this work, we investigate the impact of cholesterol in the lipid bilayer on the binding of potassium ions with gA channel and the transport of the ions across the channel. The results indicate that cholesterol can significantly influence the conformational stability of the gA channel and cause the channel deformation which inhibits the potassium ion binding with the channel and transport across the channel. The work provides some molecular insights into understanding the influence of lipids on the activity of gA channel in both model membranes and plasma membranes of intact cells.
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