0000000000732414
AUTHOR
Matthieu Réfrégiers
Binding site of different tannins on a human salivary proline-rich protein evidenced by dissociative photoionization tandem mass spectrometry
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.
Application of VUV synchroton radiation to proteomic and analytical mass spectrometry
Application of VUV synchroton radiation to proteomic and analytical mass spectrometry. 11. international conference on Synchroton radiation instrumentation (Sri 2012)
Combination of acoustic levitation with small angle scattering techniques and synchrotron radiation circular dichroism. Application to the study of protein solutions
Abstract Background The acoustic levitation technique is a useful sample handling method for small solid and liquids samples, suspended in air by means of an ultrasonic field. This method was previously used at synchrotron sources for studying pharmaceutical liquids and protein solutions using x-ray diffraction and small angle x-ray scattering (SAXS). Methods In this work we combined for the first time this containerless method with small angle neutron scattering (SANS) and synchrotron radiation circular dichroism (SRCD) to study the structural behavior of proteins in solutions during the water evaporation. SANS results are also compared with SAXS experiments. Results The aggregation behavi…