Alamethicin is an amphipathic alpha-helical peptide that forms ion channels. An early event in channel formation is believed to be the binding of alamethicin to the surface of a lipid bilayer. Molecular dynamics simulations are used to compare the structural and dynamic properties of alamethicin in water and alamethicin bound to the surface of a phosphatidylcholine bilayer. The bilayer surface ...

At submicromolar concentrations, capsaicin specifically activates the TRPV1 receptor involved in nociception. At micro- to millimolar concentrations, commonly used in clinical and in vitro studies, capsaicin also modulates the function of a large number of seemingly unrelated membrane proteins, many of which are similarly modulated by the capsaicin antagonist capsazepine. The mechanism(s) under...

The membrane of human red blood cells is essentially composed of two parts, the lipid bilayer and the membrane skeleton that interacts with the lipid bilayer. The normal resting shape of the red blood cells at physiological pH 7.4 is the discocyte. However, at alkaline pH approximately equal to 11 the shape of red blood cells is composed of a spherical parent cell and large spherical daughter v...

The reasons for lipid diversity in membranes are not understood. Here we review evidence supporting the proposal that factors related to the polymorphic capabilities of lipids provide a rationale for lipid diversity. In particular, the ability of lipids to adopt different polymorphic phases appears to be related to a generalized shape property, where lipids with a cylindrical geometry preferent...

Lattice dynamics techniques are used to simulate the orientational dynamics of the hydrophobic probe molecules 1,6-diphenyl-1,3,5-hexatriene DPH and perylene in lipid bilayer systems. It is shown that these molecules are essentially found in two distinct environments: in the middle of the bilayer and in the two regions near the bilayer interfaces. This partition arises from the competition betw...

Phosphatidylinositol-4,5-bisphosphate (PIP2), which constitutes ∼1% of the plasma membrane phospholipid, plays a key role in membrane-delimited signaling. PIP2 regulates structurally and functionally diverse membrane proteins, including voltage- and ligand-gated ion channels, inwardly rectifying ion channels, transporters, and receptors. In some cases, the regulation is known to involve specifi...