Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation

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Abstract

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.

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Noble Jesus, C., Evans, R., Forth, J., Estarellas, C., Gervasio, F. L., & Battaglia, G. (2021). Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation. ACS Macro Letters, 10(8), 984–989. https://doi.org/10.1021/acsmacrolett.1c00142

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