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Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation.

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.

SUBMITTER: Noble Jesus C

PROVIDER: S-EPMC8375021 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature

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Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation.

Noble Jesus Carlos C Evans Rhys R Forth Joe J Estarellas Carolina C Gervasio Francesco Luigi FL Battaglia Giuseppe G

ACS macro letters 20210715 8

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 physiologica ...[more]

PMID: 34422455

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