Membrane Elastic Deformations Modulate Gramicidin A Transbilayer Dimerization and Lateral Clustering.

ABSTRACT: Gramicidin A (gA) is a short β-helical peptide known to form conducting channels in lipid membranes because of transbilayer dimerization. The gA conducting dimer, being shorter than the lipid bilayer thickness, deforms the membrane in its vicinity, and the bilayer elastic energy contributes to the gA dimer formation energy. Likewise, membrane incorporation of a gA monomer, which is shorter than the lipid monolayer thickness, creates a void, thereby forcing surrounding lipid molecules to tilt to fill it. The energy of membrane deformation was calculated in the framework of the continuum elasticity theory, taking into account splay, tilt, lateral stretching/compression, Gaussian splay deformations, and external membrane tension. We obtained the interaction energy profiles for two gA monomers

SUBMITTER: Kondrashov OV 

PROVIDER: S-EPMC6084527 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature