Substitution at the C-3 Position of Catechins Has an Influence on the Binding Affinities against Serum Albumin
AbstractIt 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. View Full-Text
- Supplementary File 1:
PDF-Document (PDF, 548 KB)
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
Ikeda, M.; Ueda-Wakagi, M.; Hayashibara, K.; Kitano, R.; Kawase, M.; Kaihatsu, K.; Kato, N.; Suhara, Y.; Osakabe, N.; Ashida, H. Substitution at the C-3 Position of Catechins Has an Influence on the Binding Affinities against Serum Albumin. Molecules 2017, 22, 314.
Ikeda M, Ueda-Wakagi M, Hayashibara K, Kitano R, Kawase M, Kaihatsu K, Kato N, Suhara Y, Osakabe N, Ashida H. Substitution at the C-3 Position of Catechins Has an Influence on the Binding Affinities against Serum Albumin. Molecules. 2017; 22(2):314.Chicago/Turabian Style
Ikeda, Masaki; Ueda-Wakagi, Manabu; Hayashibara, Kaori; Kitano, Rei; Kawase, Masaya; Kaihatsu, Kunihiro; Kato, Nobuo; Suhara, Yoshitomo; Osakabe, Naomi; Ashida, Hitoshi. 2017. "Substitution at the C-3 Position of Catechins Has an Influence on the Binding Affinities against Serum Albumin." Molecules 22, no. 2: 314.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.