2020 EJRNL PP Barbara B. Gerbelli - 1.pdf
Terbatas Irwan Sofiyan
» ITB
Terbatas Irwan Sofiyan
» ITB
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.