As an alternative to meat, legumes, which are also rich in proteins, represent a promising alternative to fulfil both agri-environmental issues and feeding the planet. The faba bean (Vicia faba) is one of the most grown legume crops in France. Despite its protein richness, several locks remain to its use and consumption. The main issue is the high number of secondary metabolites that alter organoleptic and techno-functional properties of faba bean derived products. Numerous polyphenols such as flavan-3-ols monomers (catechin, epicatechin and galloyl derivatives) and oligomers (procyanidins) were detected in faba bean methanolic extract [1]. Procyanidins are responsible for the astringency due to their high reactivity and strong interaction with proteins with which they will form conjugates and complexes (i.e., tanning properties) and thus restrict protein bioavailability. Alkaline conditions often used to purify proteins from legumes lead to autoxidation of polyphenols to form quinones and other reactive intermediates that strongly increase the overall reactivity of polyphenols with proteins. If it is known that multiple factors (temperature, pH and conformation/type) determine polyphenol-proteins interactions through both non-covalent (H-bonding, electrostatic interaction, hydrophobic interaction) and covalent bond [2], little is known about the relevance of the polyphenolic pool oxidative status on the protein-polyphenols interactions determinism. Here, faba bean polyphenols are obtained through ethanolic, methanolic, acetonic or mixed solvents and their profile are elucidated using UPLC-DAD-MS. Then, major compounds will be submitted to controlled oxidation and put with globulins (the main faba bean proteins [3]) to elucidate the polyphenol oxidation relevance in the polyphenol-protein interactions.