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

研究成果: Article

6 引用 (Scopus)

抜粋

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.

元の言語English
記事番号314
ジャーナルMolecules
22
発行部数2
DOI
出版物ステータスPublished - 2017 2 1

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ASJC Scopus subject areas

  • Medicine(all)
  • Organic Chemistry

これを引用

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