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Fast Self-Assembly Dynamics of a ß-Sheet Peptide Soft Material.
Bertouille, Jolien; Kasas, Sandor; Martin, Charlotte; Hennecke, Ulrich; Ballet, Steven; Willaert, Ronnie G.
Afiliação
  • Bertouille J; Research Group of Organic Chemistry, Vrije Universiteit Brussel, Brussels, 1050, Belgium.
  • Kasas S; Laboratory of Biological Electron Microscopy, Ecole Polytechnique Fédérale de Lausanne, Lausanne, 1015, Switzerland.
  • Martin C; International Joint Research Group VUB-EPFL BioNanotechnology & NanoMedicine, Vrije Universiteit Brussel, Brussels, 1050, Belgium.
  • Hennecke U; Research Group of Organic Chemistry, Vrije Universiteit Brussel, Brussels, 1050, Belgium.
  • Ballet S; Research Group of Organic Chemistry, Vrije Universiteit Brussel, Brussels, 1050, Belgium.
  • Willaert RG; Research Group of Organic Chemistry, Vrije Universiteit Brussel, Brussels, 1050, Belgium.
Small ; 19(20): e2206795, 2023 05.
Article em En | MEDLINE | ID: mdl-36807731
ABSTRACT
Peptide-based hydrogels are promising biocompatible materials for wound healing, drug delivery, and tissue engineering applications. The physical properties of these nanostructured materials depend strongly on the morphology of the gel network. However, the self-assembly mechanism of the peptides that leads to a distinct network morphology is still a subject of ongoing debate, since complete assembly pathways have not yet been resolved. To unravel the dynamics of the hierarchical self-assembly process of the model ß-sheet forming peptide KFE8 (Ac-FKFEFKFE-NH2 ), high-speed atomic force microscopy (HS-AFM) in liquid is used. It is demonstrated that a fast-growing network, based on small fibrillar aggregates, is formed at a solid-liquid interface, while in bulk solution, a distinct, more prolonged nanotube network emerges from intermediate helical ribbons. Moreover, the transformation between these morphologies has been visualized. It is expected that this new in situ and in real-time methodology will set the path for the in-depth unravelling of the dynamics of other peptide-based self-assembled soft materials, as well as gaining advanced insights into the formation of fibers involved in protein misfolding diseases.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeos / Nanoestruturas Idioma: En Revista: Small Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeos / Nanoestruturas Idioma: En Revista: Small Ano de publicação: 2023 Tipo de documento: Article