Substitution at the C-3 position of catechins has an influence on the binding affinities against serum albumin

Masaki Ikeda, Manabu Ueda-Wakagi, Kaori Hayashibara, Rei Kitano, Masaya Kawase, Kunihiro Kaihatsu, Nobuo Kato, Yoshitomo Suhara, Naomi Osakabe, Hitoshi Ashida

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6 Citations (Scopus)

Abstract

It is known that catechins interact with the tryptophan (Trp) residue at the drug-binding site of serum albumin. In this study, we used catechin derivatives to investigate which position of the catechin structure strongly influences the binding affinity against bovine serum albumin (BSA) and human serum albumin (HSA). A docking simulation showed that (-)-epigallocatechin gallate (EGCg) interacted with both Trp residues of BSA (one at drug-binding site I and the other on the molecular surface), mainly by π-π stacking. Fluorescence analysis showed that EGCg and substituted EGCg caused a red shift of the peak wavelength of Trp similarly to warfarin (a drug-binding site I-specific compound), while 3-O-acyl-catechins caused a blue shift. To evaluate the binding affinities, the quenching constants were determined by the Stern-Volmer equation. A gallate ester at the C-3 position increased the quenching constants of the catechins. Against BSA, acyl substitution increased the quenching constant proportionally to the carbon chain lengths of the acyl group, whereas methyl substitution decreased the quenching constant. Against HSA, neither acyl nor methyl substitution affected the quenching constant. In conclusion, substitution at the C-3 position of catechins has an important influence on the binding affinity against serum albumin.

Original languageEnglish
Article number314
JournalMolecules
Volume22
Issue number2
DOIs
Publication statusPublished - 2017 Feb 1

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Keywords

  • Catechin
  • Docking study
  • Fluorescence analysis
  • Interaction
  • Serum albumin

ASJC Scopus subject areas

  • Medicine(all)
  • Organic Chemistry

Cite this

Ikeda, M., Ueda-Wakagi, M., Hayashibara, K., Kitano, R., Kawase, M., Kaihatsu, K., ... Ashida, H. (2017). Substitution at the C-3 position of catechins has an influence on the binding affinities against serum albumin. Molecules, 22(2), [314]. https://doi.org/10.3390/molecules22020314