6533b7d7fe1ef96bd1267a24
RESEARCH PRODUCT
Binding site of different tannins on a human salivary proline-rich protein evidenced by dissociative photoionization tandem mass spectrometry
Alexandre GiulianiSarah PloyonSarah PloyonSarah PloyonJean-paul MazauricJean-paul MazauricJean-paul MazauricFrancis CanonFrancis CanonFrancis CanonMatthieu RéfrégiersVéronique CheynierVéronique CheynierVéronique CheynierPascale Sarni-manchadoPascale Sarni-manchadoPascale Sarni-manchadosubject
Mass spectrometryAstringency[CHIM.ORGA]Chemical Sciences/Organic chemistry[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionOrganic ChemistryGallatePhotoionizationEpigallocatechin gallateDegree of polymerizationMass spectrometryTandem mass spectrometryBiochemistryPro line-rich proteinsBinding sitechemistry.chemical_compoundchemistryProanthocyanidinBiochemistry[ CHIM.ORGA ] Chemical Sciences/Organic chemistryDrug DiscoveryBinding siteTannins[SDV.AEN]Life Sciences [q-bio]/Food and NutritionNon-covalent interactiondescription
Abstract The sensation of astringency is thought to originate from the interaction occurring between tannins and the salivary proline-rich proteins (PRPs). Astringency perception can be modified by the structure of tannins. Herein, we study the interactions occurring between the human salivary PRP, IB5, and three model tannins with different structure, epigallocatechin gallate and the procyanidin dimers B2 and B2 3′ O -gallate, using the coupling of mass spectrometry and VUV-synchrotron radiation. The results obtained indicate that the structure of tannins, in particular the degree of polymerization and the galloylation, does not modify the binding site on IB5 involved in the interaction.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2015-05-01 |