title: Interaction between Wine Phenolic Acids and Salivary Proteins by Saturation-Transfer Difference Nuclear Magnetic Resonance Spectroscopy (STD-NMR) and Molecular Dynamics Simulations.
abstract: 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 IB712have 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.
authors.affiliation: Grupo de Investigación en Polifenoles, Unidad de Nutrición y Bromatologı́a, Facultad de Farmacia, University of Salamanca , 37007 Salamanca, Spain.|VITEC , Parc Tecnològic del Vi, 43730 Falset (Tarragona), Spain.
authors.forename: Raúl
authors.initials: R
authors.lastname: Ferrer-Gallego
authors.affiliation: Food Colour and Quality Laboratory, Department of Nutrition and Food Science, Facultad de Farmacia, Universidad de Sevilla , 41012 Sevilla, Spain.
authors.forename: José Miguel
authors.identifier: http://orcid.org/0000-0002-2329-3024
authors.initials: JM
authors.lastname: Hernández-Hierro
authors.affiliation: UCIBIO, REQUIMTE, Departamento de Quı́mica e Bioquı́mica, Faculdade de Ciências, Universidade do Porto , Rua do Campo Alegre s/n, 4169-007 Porto, Portugal.
authors.forename: Natércia F
authors.initials: NF
authors.lastname: Brás
authors.affiliation: UCIBIO, REQUIMTE, Departamento de Quı́mica e Bioquı́mica, Faculdade de Ciências, Universidade do Porto , Rua do Campo Alegre s/n, 4169-007 Porto, Portugal.
authors.forename: Nuno
authors.initials: N
authors.lastname: Vale
authors.affiliation: UCIBIO, REQUIMTE, Departamento de Quı́mica e Bioquı́mica, Faculdade de Ciências, Universidade do Porto , Rua do Campo Alegre s/n, 4169-007 Porto, Portugal.
authors.forename: Paula
authors.initials: P
authors.lastname: Gomes
authors.affiliation: LAQV-REQUIMTE, Departamento de Quı́mica e Bioquı́mica, Faculdade de Ciências, Universidade do Porto , 4169-007 Porto, Portugal.
authors.forename: Nuno
authors.initials: N
authors.lastname: Mateus
authors.affiliation: LAQV-REQUIMTE, Departamento de Quı́mica e Bioquı́mica, Faculdade de Ciências, Universidade do Porto , 4169-007 Porto, Portugal.
authors.forename: Victor
authors.initials: V
authors.lastname: de Freitas
authors.affiliation: Food Colour and Quality Laboratory, Department of Nutrition and Food Science, Facultad de Farmacia, Universidad de Sevilla , 41012 Sevilla, Spain.
authors.forename: Francisco J
authors.identifier: http://orcid.org/0000-0002-3849-8284
authors.initials: FJ
authors.lastname: Heredia
authors.affiliation: Grupo de Investigación en Polifenoles, Unidad de Nutrición y Bromatologı́a, Facultad de Farmacia, University of Salamanca , 37007 Salamanca, Spain.
authors.forename: María Teresa
authors.identifier: http://orcid.org/0000-0001-6875-2565
authors.initials: MT
authors.lastname: Escribano-Bailón
mesh_terms: D006801:Humans; D062385:Hydroxybenzoates / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D056004:Molecular Dynamics Simulation; D012471:Salivary Proteins and Peptides / Q000737:chemistry*; D013649:Taste; D014920:Wine / Q000032:analysis*
chemical_list: D062385:Hydroxybenzoates; D012471:Salivary Proteins and Peptides; C017616:phenolic acid
keywords: astringency; molecular dynamics simulations; phenolic acid; protein interaction; saturation transfer difference NMR