Interaction between Wine Phenolic Acids and Salivary Proteins by Saturation-Transfer Difference Nuclear Magnetic Resonance Spectroscopy (STD-NMR) and Molecular Dynamics Simulations

• Published in: Journal of agricultural and food chemistry Vol. 65; no. 31; pp. 6434 - 6441
• Main Authors: Ferrer-Gallego, Raúl, Hernández-Hierro, José Miguel, Brás, Natércia F, Vale, Nuno, Gomes, Paula, Mateus, Nuno, de Freitas, Victor, Heredia, Francisco J, Escribano-Bailón, María Teresa
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 09.08.2017
• Subjects: Humans; Hydroxybenzoates - chemistry; Magnetic Resonance Spectroscopy; Molecular Dynamics Simulation; Salivary Proteins and Peptides - chemistry; Taste; Wine - analysis; molecular dynamics simulations; saturation transfer difference NMR; protein interaction; phenolic acid; astringency
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/acs.jafc.6b05414

The interaction between phenolic compounds and salivary proteins is highly related to the astringency perception. Recently, it has been proven the existence of synergisms on the perceived astringency when phenolic acids were tested as mixtures in comparison to individual compounds, maintaining constant the total amount of the stimulus. The interactions between wine phenolic acids and the peptide fragment IB712 have been studied by saturation-transfer difference (STD) NMR spectroscopy. This technique provided the dissociation constants and the percentage of interaction between both individual and mixtures of hydroxybenzoic and hydroxycinnamic acids and the model peptide. It is noteworthy that hydroxybenzoic acids showed higher affinity for the peptide than hydroxycinnamic acids. To obtain further insights into the mechanisms of interaction, molecular dynamics simulations have been performed. Results obtained not only showed the ability of these compounds to interact with salivary proteins but also may justify the synergistic effect observed in previous sensory studies.