Nanofibrils are protein aggregates formed under acidic and high temperature conditions that have a long fibrous appearance due to an internal structure of stacked beta-sheets. Proteins from milk, eggs, soybean, kidney bean, and pea, can form nanofibrils when held at proper conditions, but fibrils have yet to be formed from peanut proteins. The goal of this research was to determine if nanofibrils can be formed from peanut proteins and to characterize their formation kinetics, structure and functionality. Nanofibrils were formed under different conditions as determined using ThT fluorescence and TEM imaging. Nanofibrils are characterized as having shear thinning and viscosity enhancing behavior, and varying pH solubility. Such food protein nanofibrils could be important to the food industry as they might be used to stabilize or flocculate emulsions/foams, enhance viscosity, and form gel networks at lower protein concentrations than commonly used aggregates.