Current methodologies for assessing protein–phenolic interactions

In recent years, studies have been conducted to understand the interactions between nutritional components and their potential effects on human health. Studies focusing on interactions between proteins and phenolic components have created an area of interest. In this review, the mechanism of protein–phenolic interactions and the methods used to reveal the protein–phenolic interactions are described. It has been shown that polyphenols have strong binding affinities for proteins, leading to changes in their structure and properties, and affecting the bioavailability and bioaccessibility of the polyphenols. This review systematically reviewed the diverse methods for analyzing the protein–phenolic interactions and classified them into five categories: microscopic, thermodynamic, electrophoretic and chromatographic, bioinformatics and spectroscopic. Surface and particle morphology were investigated by microscopic methods, binding and temperature stability by thermodynamic methods, covalent and non-covalent interactions by electrophoretic and chromatographic methods, binding affinity by bioinformatics methods, and binding and complex formation by spectroscopic methods.