Organic Nanoscrolls from Electrostatic Interactions between Peptides and Lipids: Assembly Steps and Structure
| Autor: | Christophe Chassaing, Cristina Petcut, Joël Richard, Naziha Benamar, Keinny François, Damien Rault, Franck Artzner, Maité Paternostre, Cristelle Mériadec, Thomas Bizien, Pierre Chervy |
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| Přispěvatelé: | Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Interactions et mécanismes d’assemblage des protéines et des peptides (IMAPP), Département Biochimie, Biophysique et Biologie Structurale (B3S), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut de Physique de Rennes (IPR), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS), Synchrotron SOLEIL (SSOLEIL), Centre National de la Recherche Scientifique (CNRS), Ipsen [Boulogne Billancourt] (Ipsen), IPSEN, ANR and Ipsen, ANR-14-LAB5-0001,ArchiPex,Auto-Assemblage et formulations de peptides thérapeutiques(2014), ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS), Institute for Integrative Biology of the Cell (I2BC) |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Self-assembly mechanism
MESH: peptide MESH: electrostatic interactions MESH: supramolecular architectures Lipid Bilayers Static Electricity Peptide 02 engineering and technology Supramolecular architectures 010402 general chemistry Peptides Cyclic 01 natural sciences lipids Lipids packing Static electricity Electrochemistry Molecule General Materials Science [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology MESH: self-assembly Spectroscopy chemistry.chemical_classification Nanotubes MESH: lipids Cationic polymerization Phosphatidylglycerols Surfaces and Interfaces self-assembly 021001 nanoscience & nanotechnology Condensed Matter Physics Electrostatics electrostatic interactions 0104 chemical sciences [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics Membrane chemistry Biophysics peptides Self-assembly Somatostatin 0210 nano-technology |
| Zdroj: | Langmuir Langmuir, 2019, 35 (32), pp.10648-10657. ⟨10.1021/acs.langmuir.9b01542⟩ Langmuir, American Chemical Society, 2019, 35 (32), pp.10648-10657. ⟨10.1021/acs.langmuir.9b01542⟩ |
| ISSN: | 0743-7463 1520-5827 |
| DOI: | 10.1021/acs.langmuir.9b01542⟩ |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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