N- and S-homocysteinylation reduce the binding of human serum albumin to catechins.

Angelo Zinellu, Salvatore Sotgia, Bastianina Scanu, Dionigia Arru, Annalisa Cossu, Anna Posadino, Roberta Giordo, Arduino Mangoni, Gianfranco Pintus, Ciriaco Carru

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Purpose: The dietary flavonoids epicatechin (EC), epigallocatechin (EGC), epicatechin gallate (ECG) and epigallocatechin gallate (EGCG) have been shown to interact with circulating albumin for transport in blood to different body tissues. This interaction may modulate their bioavailability and effectiveness. Methods: Using affinity capillary electrophoresis to assess binding constants (K b ), we investigated whether posttranslational modification of human serum albumin (HSA) through N- and S-homocysteinylation, commonly observed in hyperhomocysteinemia, may modify its interaction with catechins. Results: S-Hcy HSA had lower K b values toward EC (14 %), EGC (18 %), ECG (24 %) and EGCG (30 %). Similarly, N-Hcy HSA had lower K b values toward EC (17 %), EGC (22 %), ECG (23 %) and EGCG (32 %). No differences were observed in the affinity between catechins, albumin and mercaptalbumin. Conclusion: Therefore, HSA posttranslational modifications typical of hyperhomocysteinemia reduce its affinity to catechins, potentially affecting their pharmacokinetics and availability at the active sites.

Original languageEnglish
Pages (from-to)785-791
Number of pages7
JournalEuropean Journal of Nutrition
Volume56
Issue number2
DOIs
Publication statusPublished - 1 Mar 2017

Keywords

  • Affinity capillary electrophoresis
  • Albumin
  • Binding constant
  • Catechins

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