Litcius/Paper detail

Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation

Carlos Noble Jesus, Rhys Evans, Joe Forth, Carolina Estarellas, Francesco Luigi Gervasio, Giuseppe Battaglia

2021ACS Macro Letters14 citationsDOIOpen Access PDF

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
Amphiphilic Histidine-Based Oligopeptides Exhibit pH-Reversible Fibril Formation | Litcius