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Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation

[Image: see text] We report the design, simulation, synthesis, and reversible self-assembly of nanofibrils using polyhistidine-based oligopeptides. The inclusion of aromatic amino acids in the histidine block produces distinct antiparallel β-strands that lead to the formation of amyloid-like fibrils...

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Detalles Bibliográficos
Autores principales: Noble Jesus, Carlos, Evans, Rhys, Forth, Joe, Estarellas, Carolina, Gervasio, Francesco Luigi, Battaglia, Giuseppe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8375021/
https://www.ncbi.nlm.nih.gov/pubmed/34422455
http://dx.doi.org/10.1021/acsmacrolett.1c00142
Descripción
Sumario:[Image: see text] We report the design, simulation, synthesis, and reversible self-assembly of nanofibrils using polyhistidine-based oligopeptides. The inclusion of aromatic amino acids in the histidine block produces distinct antiparallel β-strands that lead to the formation of amyloid-like fibrils. The structures undergo self-assembly in response to a change in pH. This creates the potential to produce well-defined fibrils for biotechnological and biomedical applications that are pH-responsive in a physiologically relevant range.