ABSTRACTThe interaction between plant proteins and dietary polyphenols has garnered significant interest due to its impact on the structural, functional, and digestibility properties of proteins. This review explores the mechanisms underlying protein–polyphenol interactions, including noncovalent (hydrogen bonding, hydrophobic interactions, and electrostatic forces) and covalent bonding, and their implications on structural and functional properties of proteins and their digestibility. Various factors influencing these interactions, such as polyphenol structure, protein composition, temperature, and pH, are discussed. The review examines data on the impact of polyphenols on protein digestibility, shedding light on the mechanisms underlying these modifications and emphasizing the need for a thorough understanding of these processes. It further highlights the role of polyphenols on digestive enzymes, which can either enhance or hinder their enzymatic activities. A structural and molecular levels elucidation of these interactions provides valuable insights for enhancing the functionality and efficacy of plant‐based proteins in food applications.