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The Role of Amylogenic Fiber Aggregation on the Elasticity of a Lipid Membrane.

This work presents a systematic study of the swelling behavior of a lecithin lamellar phase incorporating different amounts of the short peptide sequence diphenylalanine (FF). Small- and wide-angle X-ray scattering assays provide relevant information about the structure and elasticity of the lamellar stacking. These data show that important changes occur at the interface of the lipid membrane dependent not only on the peptide content but also on the hydration of the lamellar structure. Multilamellar-to-unilamellar transitions, previously observed for an increasing number of peptides, are now observed to be dependent on the hydration of the lamellar phase. Wide-angle X-ray scattering and electron microscopy observations (TEM) provide experimental evidence of peptide aggregation into long amylogenic fibers. We argue that aggregates that partition in water may become large enough to destabilize the lamellar structure. It is also shown that, for a given peptide concentration, the lamellar structure can be rendered more flexible or more rigid, by tuning the hydration.