Amyloidogenic proteins undergo an alternative folding pathway under stressful conditions leading to formation of fibril products, presenting cross β-sheet structure which is the hallmark of many neurodegenerative diseases. The current work demonstrates the effectiveness of phloridzin small molecule on the inhibition of hen egg white lysozyme (HEWL) amyloid formation. The inhibitory effects were analyzed by thioflavin T-induced fluorescence, circular dichroism, and atomic force microscopy. This report demonstrated that naturally occurring small molecules may serve a function that is typically done by protein chaperones, and it provides a hint for designing inhibitors against amyloid formation products associated with neurodegenerative diseases. This report showed that phloridzin considerably hindered nucleation, and therefore, FIBRILLATION of lysozyme in a dose-dependent manner.