Correlation between the effects of a cationic peptide on the hydration and fluidity of anionic lipid bilayers: a...

The cationic tridecapeptide alpha-melanocyte stimulating hormone (alpha-MSH) is known to interact with anionic vesicles of 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG), partially penetrating the lipid membrane. In the lipid liquid crystal phase, phospholipid derivatives spin labeled at the different C-atoms along the acyl chain, show that the peptide increases the bilayer packing at all depths. Parallel to that, there is an increase in the probe's isotropic hyperfine splittings, indicating that the peptide significantly decreases the membrane hydrophobic barrier. Accordingly, it is suggested that the increase in membrane packing yielded by alpha-MSH is partly due to a greater level of interchain hydration. This result is compared to the increase in packing and decrease in polarity yielded by cholesterol, and the absence of structural or polar alterations with Na+. The latter result shows that the peptide effect is not related to an increase of positive charges at the anionic vesicle surface. Alterations on the lipid bilayer polar profile measured by the nitroxide hyperfine splitting z component in frozen samples are shown to be different from those obtained at room temperature. However, it is shown here that a certain correlation can be drawn between the increase in polarity measured in frozen samples and the packing effect caused by the different molecules in the lipid gel phase.