Related Experiment Video
Updated: Nov 30, 2025

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
Published on: March 17, 2010
Interactions between polyphenol oxidation products and salivary proteins: Specific affinity of CQA dehydrodimers with
Claudia Mariana Castillo-Fraire1, Elsa Brandão2, Pascal Poupard3
1INRAE UR BIA - Polyphenols, Reactivity, Processes, F-35653 Le Rheu, France; UMT ACTIA Nova(2)Cidre, F-35653 Le Rheu, France.
Abstract:
Throughout the apple juice and cider making process, polyphenols undergo enzymatic oxidation which generates a great variety of polyphenol oxidation products. Since 5'-O-Caffeoylquinic acid (CQA) is one of the major phenolic compounds and the preferential substrate for polyphenoloxidase in apple juice, its oxidation leads to the formation of newly formed molecules by which dehydrodimers (MW 706 Da) are included. Interactions of salivary proteins (SP) with native polyphenols is a well-known phenomenon, but their interactions with polyphenol oxidation products has not been studied yet. In this work, we decided to decipher the interactions between CQA dehydrodimers and SP (gPRPs, aPRPs, statherins/P-B peptide, and cystatins) using HPLC-UV and fluorescence. These results showed that contrary to what was expected, CQA dehydrodimers presented a low interaction with PRPs, but revealed a specific interaction with statherins/P-B peptide and cystatins. This work settles for the first time the interactions between SP and polyphenol oxidation products.
More Related Videos
08:37Sampling Human Indigenous Saliva Peptidome Using a Lollipop-Like Ultrafiltration Probe: Simplify and Enhance Peptide Detection for Clinical Mass Spectrometry
Published on: August 7, 2012
07:16Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021