Shear-induced structure and mechanics of β-lactoglobulin amyloid fibrils

Abstract

Alzheimer first identified amyloid plaques during autopsies of the brains of dementia patients in 1905. Considerable effort has since been directed to understanding the composition, structure and formation mechanism of amyloid fibrils. A variety of proteins have now been shown to self-assemble into amyloid fibrils. Furthermore, the association between misfolded proteins and a wide range of diseases is now established. Here we examine the effect of shear on the formation, structure and mechanical properties of amyloid fibrils. Atomic force microscopy is used to both image and measure the nanomechanical properties of β-lactoglobulin (β-Lg) amyloid fibrils generated in controlled (Couette) and ..