Binding affinity of tea catechins for HSA: Characterization by high-performance affinity chromatography with immobilized albumin column

Takeshi Ishii, Kanako Minoda, Min Jung Bae, Taiki Mori, Yoshinori Uekusa, Tatsuya Ichikawa, Yoshiyuki Aihara, Takumi Furuta, Toshiyuki Wakimoto, Toshiyuki Kan, Tsutomu Nakayama

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Catechins are the major polyphenols in green tea leaves. Recent studies have suggested that the catechins form complexes with HSA for transport in human blood, and their binding affinity for albumin is believed to modulate their bioavailability. In this study, the binding affinities of catechins and their analogs were evaluated and the relationship between the chemical structure of each catechin and its binding property were investigated. Comparing these catechins by HPLC analysis with the HSA column, we showed that galloylated catechins have higher binding affinities with HSA than non-galloylated catechins. In addition, pyrogallol-type catechins have a high affinity compared to catechol-type catechins. Furthermore, the binding affinity of the catechin with 2,3-trans structure was higher than those of the catechin with 2,3-cis structure. The importance of the hydroxyl group on the galloyl group and B-ring was confirmed using methylated catechins. These results indicate that the most important structural element contributing to HSA binding of tea catechins is the galloyl group, followed by the number of hydroxyl groups on the B-ring and the galloyl group or the configuration at C-2. Our findings provide fundamental information on the relationship between the chemical structure of tea catechins and its biological activity.

Original languageEnglish
Pages (from-to)816-822
Number of pages7
JournalMolecular Nutrition and Food Research
Volume54
Issue number6
DOIs
Publication statusPublished - 2010 Jun

Keywords

  • Binding affinity
  • Chemical structure
  • Galloyl group
  • HSA
  • Tea catechin

ASJC Scopus subject areas

  • Biotechnology
  • Food Science

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    Ishii, T., Minoda, K., Bae, M. J., Mori, T., Uekusa, Y., Ichikawa, T., Aihara, Y., Furuta, T., Wakimoto, T., Kan, T., & Nakayama, T. (2010). Binding affinity of tea catechins for HSA: Characterization by high-performance affinity chromatography with immobilized albumin column. Molecular Nutrition and Food Research, 54(6), 816-822. https://doi.org/10.1002/mnfr.200900071