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- W3129691540 abstract "Specific sections of amyloid proteins, present in diseases such as Alzheimer's and Parkinson's, have recently inspired the design of peptides that self-assemble into supramolecular nanostructures. This work presents novel amyloid-like amphiphilic peptides that self-assemble into robust fibers with a beta-sheet like structure, in which the self-assembly is driven by π-stacking of aromatic residues placed at specific locations of the peptides. Different amyloid-like peptides have been designed in order to study how additional negatively charged residues at both ends of the sequence affect the morphology of the supramolecular structures. The molecular-level features of these assemblies have been predicted through Coarse-Grained Molecular Dynamics simulations, selecting those suitable for applications in biomedicine and nanotechnology. The selected fibers have been characterized experimentally using biophysical techniques to assess their morphological features. The synergy of both approaches has provided us with a level of understanding of our system which will allow further rational modifications of the sequence in order to modify its structure and functionality." @default.
- W3129691540 created "2021-03-01" @default.
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- W3129691540 date "2021-02-01" @default.
- W3129691540 modified "2023-09-25" @default.
- W3129691540 title "A Multidisciplinary Approach to Design Amyloid-Like Peptides to Form Supramolecular Assemblies" @default.
- W3129691540 doi "https://doi.org/10.1016/j.bpj.2020.11.1418" @default.
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