Effects of Incubation Temperature on Nanomechanical Properties of β-Lactoglobulin Amyloid Fibers

Amyloid fibrils constitute a class of highly ordered nanomaterials formed by aggregates of the protein. Although The irreversible fibril formation of various proteins is related to the disorders like Alzheimer’s diseases, Creutzfeldt-Jacob and many more, amyloid fibrils have also been noticed in many physiologically beneficial roles such as in adhesive and hormone storage. Here, we compare the stiffness and structural properties of the amyloid fibers examined by the statistical approaches of single molecule atomic force microscopy images of heat-denatured β-lactoglobulin fibrils at different incubation time period (24, 48, and 72 hours). We demonstrate the gradual decrease in stiffness of the fibril with time without any change in dimension of each monomer