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

Research output: Contribution to journalArticle

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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.

LanguageEnglish
Article number314
JournalMolecules
Volume22
Issue number2
DOIs
StatePublished - 2017 Feb 1

Fingerprint

Catechin
Serum Albumin
Substitution reactions
Quenching
Bovine Serum Albumin
Tryptophan
Binding Sites
Pharmaceutical Preparations
Warfarin
Chain length
Esters
Carbon
Fluorescence
Derivatives
Wavelength
epigallocatechin gallate

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]. DOI: 10.3390/molecules22020314

Substitution at the C-3 position of catechins has an influence on the binding affinities against serum albumin. / Ikeda, Masaki; Ueda-Wakagi, Manabu; Hayashibara, Kaori; Kitano, Rei; Kawase, Masaya; Kaihatsu, Kunihiro; Kato, Nobuo; Suhara, Yoshitomo; Osakabe, Naomi; Ashida, Hitoshi.

In: Molecules, Vol. 22, No. 2, 314, 01.02.2017.

Research output: Contribution to journalArticle

Ikeda, M, Ueda-Wakagi, M, Hayashibara, K, Kitano, R, Kawase, M, Kaihatsu, K, Kato, N, Suhara, Y, Osakabe, N & Ashida, H 2017, 'Substitution at the C-3 position of catechins has an influence on the binding affinities against serum albumin' Molecules, vol 22, no. 2, 314. DOI: 10.3390/molecules22020314
Ikeda M, Ueda-Wakagi M, Hayashibara K, Kitano R, Kawase M, Kaihatsu K et al. Substitution at the C-3 position of catechins has an influence on the binding affinities against serum albumin. Molecules. 2017 Feb 1;22(2). 314. Available from, DOI: 10.3390/molecules22020314
Ikeda, Masaki ; Ueda-Wakagi, Manabu ; Hayashibara, Kaori ; Kitano, Rei ; Kawase, Masaya ; Kaihatsu, Kunihiro ; Kato, Nobuo ; Suhara, Yoshitomo ; Osakabe, Naomi ; Ashida, Hitoshi. / Substitution at the C-3 position of catechins has an influence on the binding affinities against serum albumin. In: Molecules. 2017 ; Vol. 22, No. 2.
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