This article investigates the structure and emulsification properties of peanut protein amyloid fibrils (PAFs) formed at pH 2.0 and different protein concentrations (PC).The findings demonstrated that with an escalation in the PC concentration (10-80 mg/mL), the conversion rate and β-sheet ratio of the fibrils significantly rose, suggesting that the increase in protein concentration promoted the formation of the fibrils.When the concentration was 10 mg/mL, large aggregates and a few short fibrils were formed; when the concentration was 40 mg/mL, more curved fibrils were formed; when the concentration is 60 mg/mL, long curved fibrils were formed; at higher concentrations (80 mg/mL), short and thick fibrils and rigid straight fibrils were formed.This indicates that the morphol. of the fibrils formed under different PCs varies.Addnl., increasing the concentration of PC (10-60 mg/mL) rendered the PAF structure more stable, enhanced the thermal stability, and resulted in a higher emulsification activity index (EAI).When the protein concentration was higher (80 mg/mL), the EAI of the fibrils decreased.This study will intensify the exploration of the concentration-regulated protein fibrillation.