Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation
Carlos Noble Jesus, Rhys Evans, Joe Forth, Carolina Estarellas, Francesco Luigi Gervasio, Giuseppe Battaglia
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.
Topics & Concepts
Antiparallel (mathematics)HistidineOligopeptideAmphiphileFibrilAmyloid fibrilSelf-assemblyChemistryAmino acidAmyloid (mycology)BiophysicsMaterials sciencePeptideOrganic chemistryCopolymerBiochemistryPolymerAmyloid βInorganic chemistryMagnetic fieldMedicineBiologyDiseasePhysicsQuantum mechanicsPathologySupramolecular Self-Assembly in MaterialsPolydiacetylene-based materials and applicationsLuminescence and Fluorescent Materials