Real‐Time Analysis of Polyphenol–Protein Interactions by Surface Plasmon Resonance Using Surface‐Bound Polyphenols. Issue 17 (24th February 2021)

• Record Type: Journal Article
• Authors: Delannoy López, Daniela Mélanie; Tran, Dong Tien; Viault, Guillaume; Dairi, Sofiane; Peixoto, Philippe Alexandre; Capello, Yoan; Minder, Laëtitia; Pouységu, Laurent; Génot, Elisabeth; Di Primo, Carmelo; Deffieux, Denis; Quideau, Stéphane
• Is Part Of: Chemistry. Volume 27:Issue 17(2021)
• Page Start: 5498
• Page End: 5508
• Publication Date: 2021-02-24
• Subjects: analytical methods -- immobilization -- polyphenols -- proteins -- surface plasmon resonance; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.202005187
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract: A selection of bioactive polyphenols of different structural classes, such as the ellagitannins vescalagin and vescalin, the flavanoids catechin, epicatechin, epigallocatechin gallate (EGCG), and procyanidin B2, and the stilbenoids resveratrol and piceatannol, were chemically modified to bear a biotin unit for enabling their immobilization on streptavidin‐coated sensor chips. These sensor chips were used to evaluate in real time by surface plasmon resonance (SPR) the interactions of three different surface‐bound polyphenolic ligands per sensor chip with various protein analytes, including human DNA topoisomerase IIα, flavonoid leucoanthocyanidin dioxygenase, B‐cell lymphoma 2 apoptosis regulator protein, and bovine serum albumin. The types and levels of SPR responses unveiled major differences in the association, or lack thereof, and dissociation between a given protein analyte and different polyphenolic ligands. Thus, this multi‐analysis SPR technique is a valuable methodology to rapidly screen and qualitatively compare various polyphenol–protein interactions. Abstract : SPR sensor chips : Seven plant polyphenols of four different structural classes (ellagitannins, flavanols, proanthocyanidins, and stilbenoids) were synthesized and/or chemically modified at selected carbon centers for enabling their biotinylation and subsequent immobilization in order to examine their interactions with various proteins in real time by surface plasmon resonance (SPR) on streptavidin‐coated sensor chips. The SPR responses unveiled major differences in the modes of association and dissociation of these polyphenol–protein interactions.