Gerbelli Barbara B, Ly Isabelle, Pedemay Sandra, Alves Wendel A, de Oliveira Elisabeth A
Centro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André 09210-580, Brazil.
Centre de Recherche Paul Pascal, University of Bordeau, 33600 Pessac, France.
ACS Appl Bio Mater. 2020 Feb 17;3(2):815-822. doi: 10.1021/acsabm.9b00861. Epub 2020 Jan 30.
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.
这项工作对掺入不同量短肽序列二苯基丙氨酸（FF）的卵磷脂层状相的溶胀行为进行了系统研究。小角和广角X射线散射分析提供了有关层状堆积结构和弹性的相关信息。这些数据表明，脂质膜界面处发生的重要变化不仅取决于肽含量，还取决于层状结构的水合作用。先前观察到越来越多的肽会发生多层到单层的转变，现在观察到这种转变取决于层状相的水合作用。广角X射线散射和电子显微镜观察（透射电子显微镜）提供了肽聚集成淀粉样长纤维的实验证据。我们认为，在水中分配的聚集体可能会变得足够大，从而破坏层状结构的稳定性。研究还表明，对于给定的肽浓度，通过调节水合作用，可以使层状结构变得更灵活或更刚性。
