Astringency - Protein-tannins interaction: Driving forces of polyphenols-to-protein binding

6 important questions on Astringency - Protein-tannins interaction: Driving forces of polyphenols-to-protein binding

Which residues of proteins are involved in the interaction with polyphenols? And how is this called?

Proline residues are involved by so-called stacking of flat aromatic rings of the tannin to the slightly crooked pyrrolidine ring of the proline residue.

Why is proline attractive for binding tannins (or polyphenols)?

It contains 2 electropositive hydrogen atoms (Halpha and Hdelta), likely to interact with the pi-electron cloud of phenolic rings via Ch-pi stacking.

What is the difference between Halpha and Hdelta in proline?

Halpha is more favourable to interact with the phenolic ring. It has a higher electrophilicity, as it is positioned between 2 relatively electronegative regions (the N atom and the carbonyl).
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What is the result when proteins and polyphenols interact?

They precipitate from the solution.

Which 2 types of polyphenol-to-protein complexation can be distinguished?

  • Monodentate
  • Multidentate

What is the difference between monodentate and multidentate polyphenol-to-protein complexation?

  • Monodentate
    • monomeric polyphenols with relatively low affinity for proteins
    • polyphenol-to-protein molar ratio: very high --> to induce precipitation
    • polyphenols create hydrophobic shell around proteins --> aggregation --> precipitation
  • Multidentate
    • multimeric polyphenols (e.g. Proanthocyanidins or hydrolysable tannins) with high affinity for proteins
    • polyphenol-to-protein molar ratio: low
    • cross-linkers between proteins --> aggregates --> precipitation

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