Interactions between polyphenols and proteins have been studied for many decades, with a primary focus on the noncovalent, reversible complexes that form rapidly in aqueous solution.  These interactions have long attracted the interest of food and beverage scientists, since they are factors in important properties including haze formation and astringency.  Recent appreciation of the beneficial health effects of polyphenols has driven additional research into interactions with proteins that may impact bioactivity, bioavailability or analytical methodology.  For example, in the blood stream, polyphenols may inhibit or exacerbate protein glycation, changing the physiological function of both protein and polyphenol.  Interaction with protein in the gastrointestinal tract may dictate uptake of polyphenols, while interaction with serum albumin may prolong the lifetime of polyphenols after absorption.  Reaction to form covalent complexes may mask the polyphenol, making it analytically inaccessible and changing its targets and bioactivities. Unanswered questions and directions for future research will be highlighted.

Reactions between polyphenolic dietary supplements and other biomolecules dictate bioactivity, bioavailability and analysis

250th National Meeting (2015)

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