Ion-channels embedded within biological membranes help mediate the transport of ions, and by doing so help establish osmotic stasis, facilitate bioenergetics and provide the means for transmitting environmental signals. It is clear that the structural and functional properties of ion-channels are highly sensitive to the intermolecular forces that act in the bilayer.  Using molecular dynamics simulations of LS2 and LS3 homo-oligomeric bundles ranging from 1-6 peptides, we examined the lipid bilayer perturbations. We focus on the hydrophilic and hydrophobic interactions between the bundles and surrounding lipids, which are pivotal in the protein's structural orientation.  We conclude that the perturbation of the bilayer is strongest for bundle conformations consisting of 3 or less peptides.  Additionally, we observed that there is a strong correlation between the tilt angles of the helix/helices of each system with the hydrophobic mismatch of the lipid bilayer and lipid distribution.

Molecular dynamics studies on bilayer perturbations comprised of homo-oligomeric bundles

244th National Meeting (2012)

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