Sorbitol Modulates the Structure and Nanomechanics of κ-casein Amyloid Fibrils

Amyloid fibrils are highly ordered protein aggregates that, beyond their pathological roles, are increasingly recognized as functional structures in food systems. κ-casein is a particularly interesting model due to its dual relevance: it stabilizes casein micelles in milk but can also form amyloid fibrils under destabilizing conditions. In this work, we investigate how the food-grade osmolyte sorbitol modulates the fibrillation, structure, and nanomechanics of κ-casein. Thioflavin T fluorescence