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.
Highlights
We report the design, simulation, synthesis, and reversible self-assembly of nanofibrils using polyhistidine-based oligopeptides
Studies of larger oligopeptides remain beyond the reach of computational approaches, while dynamic combinatorial library approaches often provide limited fundamental insight
The design for our histidine-based peptide revolved around a diblock copeptide sequence that would be amphiphilic at neutral pH and possess antifouling properties: (EK)2-(H)[12]
Summary
Simulation, synthesis, and reversible self-assembly of nanofibrils using polyhistidine-based oligopeptides. We report the rational synthesis and self-assembly of short pH-sensitive histidine-based amphiphilic oligopeptides that produce amyloid fibril structures.
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