Abstract
Electron spin resonance spectroscopy was used to examine the interaction of the lytic polypeptide, melittin, with model membrane systems in order to determine the physical basis for its alterations of membrane properties. Sonically dispersed egg lecithin (phosphatidylcholine), phosphatidylserine, extracted Escherichia coli phospholipids, and isolated E. coli membranes were spin-labeled with fatty acid probes and treated with melittin solutions. Spectral analysis indicates that melittin induces a disruption of the phospholipid matrix without a significant change in the mobility of extensive regions of the acyl chains. This perturbation causes a melittin concentration dependent alteration in the capacity of the lipid matrix for spin label such that more of the probe is taken up. The effects are independent of phospholipid composition and the presence of membrane proteins. It is suggested that melittin participates in a hydrophobic interaction with the hydrocarbon region of the bilayer and acts as a disrupter of matrix ordering.
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