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Insights into the Binding of Dietary Phenolic Compounds to Human Serum Albumin and Food-Drug Interactions.

Anallely López-YerenaMaria PérezAnna Vallverdu-QueraltElvira Escribano-Ferrer
Published in: Pharmaceutics (2020)
The distribution of drugs and dietary phenolic compounds in the systemic circulation de-pends on, among other factors, unspecific/specific reversible binding to plasma proteins such as human serum albumin (HSA). Phenolic substances, present in plant-derived feeds, foods, beverages, herbal medicines, and dietary supplements, are of great interest due to their biological activity. Recently, considerable research has been directed at the formation of phenol-HSA complexes, focusing above all on structure-affinity relationships. The nucleophilicity and planarity of molecules can be altered by the number and position of hydroxyl groups on the aromatic ring and by hydrogenation. Binding affinities towards HSA may also differ between phenolic compounds in their native form and conjugates derived from phase II reactions. On the other hand, food-drug interactions may increase the concentration of free drugs in the blood, affecting their transport and/or disposition and in some cases provoking adverse or toxic effects. This is caused mainly by a decrease in drug binding affinities for HSA in the presence of flavonoids. Accordingly, to avoid the side effects arising from changes in plasma protein binding, the intake of flavonoid-rich food and beverages should be taken into consideration when treating certain pathologies.
Keyphrases
  • human serum albumin
  • phase ii
  • binding protein
  • clinical trial
  • dna binding
  • human health
  • open label
  • amino acid
  • risk assessment
  • drinking water
  • mass spectrometry
  • phase iii