Most natural plant proteins have dense spherical structures, reducing their functionality and accessibility to proteases, which limits their application in the food industry to some extent. The preparation of plant protein amyloid fibrils with high aspect ratio and excellent interfacial properties through acid-heat-induced self-assembly can significantly improve the physicochemical properties, nutritional value, and functional characteristics of plant proteins. This study reviews the formation mechanism and preparation methods of acid-heat-induced self-assembly of plant protein amyloid fibrils, summarizes the relationship between their structure and properties, discusses the application directions of plant protein amyloid fibrils, and looks forward to their future research directions.