V. Fodera

Insulin Amyloid Morphology is Encoded in H-bonds and Electrostatics Interactions Ruling Protein Phase Separation

The paper investigates how anion-protein interactions influence insulin phase separation and amyloid formation through H-bonds and electrostatics, revealing alternative pathways to fibril formation.

Heterogeneous and Surface-Catalyzed Amyloid Aggregation Monitored by Spatially Resolved Fluorescence and Single Molecule Microscopy

The paper uses spatially resolved fluorescence and single molecule microscopy combined with machine learning to analyze amyloid aggregation, identifying rate constants and mechanisms.

In vitro and in vivo immunogenicity assessment of protein aggregate characteristics

This study assesses the immunogenicity of human insulin aggregates with varying size, structure, and modifications, finding that flexible aggregates with altered secondary structure are most immunogenic.

Morphological integrity of insulin amyloid-like aggregates depends on preparation methods and post-production treatments

This study investigates how preparation methods and post-treatment affect the morphology and integrity of insulin amyloid-like aggregates.

Direct Observation of Heterogeneous Formation of Amyloid Spherulites in Real-time by Super-resolution Microscopy

This study uses super-resolution microscopy to observe and quantify the heterogeneous growth of amyloid spherulites in real-time, revealing anisotropic growth pathways and energy landscapes.

Polysorbate 80 Controls Morphology, Structure and Stability of Human Insulin Amyloid-Like Spherulites

This study shows that polysorbate 80 affects insulin aggregation kinetics and physicochemical properties of formed amyloid-like spherulites.

Zinc Determines Dynamical Properties and Aggregation Kinetics of Human Insulin

This study investigates how zinc affects insulin dynamics and aggregation kinetics, showing that zinc binding stabilizes insulin and modifies its aggregation behavior.