Abstract
An important aspect of cells is their shape flexibility that gives them motion but also a high adaptation versatility to their environment. This shape versatility is mediated by different types of protein-membrane interactions among which electrostatic plays an important role. In the present work we examined the interaction between a small dicationic peptide, that possesses self-assembly properties, and lipid model membranes. The peptide, lanreotide, spontaneously forms nanotubes in water that have a strictly uniform diameter. In the current work, we show that the interaction between the cationic peptide and negatively charged bilayers of lipids induces the formation of myelin sheath-like structures that we call nanoscrolls. By deciphering the different steps of formation and the molecular structure of the self-assembly, we show how electrostatics modify the spontaneous peptide and lipid way of packing.
Highlights
IntroductionMicrotubules, microfilaments, chromatin, etc., are all dynamic and functional architectures playing a crucial role in the compartmentation of cellular functions
The authors showed that the nanoscroll structures disappeared upon the addition of ethylenediamine tetraacetic acid (EDTA), a strong chelating agent for Ca2+
Lanreotide and Ca2+, the interaction is driven by strong electrostatic attraction
Summary
Microtubules, microfilaments, chromatin, etc., are all dynamic and functional architectures playing a crucial role in the compartmentation of cellular functions These functional and versatile materials have been selected by evolution, and the chemical and physicochemical rules governing their formation are yet to be understood in detail. This is of great importance in biology and for material science, as the understanding of the strategies selected by nature could be used to build de novo materials with versatile properties.[1−9] particular attention is devoted to protein assemblies because fibrillary architectures formed by misfolded proteins have been associated with diseases, in particular neurodegenerative[10] and systemic amyloidosis.[11]. This protein that forms fibers is known to interact with membranes and to play a role in the preservation of the pool of synaptic vesicles within the neuron.[14]
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