Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation

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 u...

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Bibliographic Details
Published in:ACS macro letters 2021-08, Vol.10 (8), p.984-989
Main Authors: Noble Jesus, Carlos, Evans, Rhys, Forth, Joe, Estarellas, Carolina, Gervasio, Francesco Luigi, Battaglia, Giuseppe
Format: Article
Language:English
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Letter
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Summary: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.
ISSN:2161-1653
2161-1653
DOI:10.1021/acsmacrolett.1c00142