Next Article in Journal
Special Issue: Ribosome-Inactivating Proteins—Commemorative Issue in Honor of Professor Fiorenzo Stirpe
Previous Article in Journal
Accumulation of Carotenoids and Metabolic Profiling in Different Cultivars of Tagetes Flowers
Article Menu
Issue 2 (February) cover image

Export Article

Open AccessArticle
Molecules 2017, 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

1
Graduate School of Agricultural Science, Kobe University, 1-1 Rokkodai, Nada-ku, Kobe, Hyogo 657-8501, Japan
2
National Agriculture and Food Research Organization, National Food Research Institute, Tsukuba, Ibaraki 305-8642, Japan
3
Department of Bioscience, Nagahama Institute of Bio-Science and Technology, 1266 Tamura-cho, Nagahama, Shiga 526-0829, Japan
4
Department of Organic Fine Chemicals, The Institute of Scientific and Industrial Research, Osaka University, 8-1, Mihogaoka, Ibaraki, Osaka 567-0047, Japan
5
Department of Bioscience and Engineering, College of Systems Engineering and Science, Shibaura Institute of Technology, 307 Fukasaku, Minuma-ku, Saitama 337-8570, Japan
*
Author to whom correspondence should be addressed.
Academic Editor: Thomas J. Schmidt
Received: 29 December 2016 / Revised: 15 February 2017 / Accepted: 16 February 2017 / Published: 18 February 2017
(This article belongs to the Section Natural Products)
View Full-Text   |   Download PDF [1326 KB, uploaded 18 February 2017]   |  

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. View Full-Text
Keywords: catechin; serum albumin; interaction; docking study; fluorescence analysis catechin; serum albumin; interaction; docking study; fluorescence analysis
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never 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

SciFeed Share & Cite This Article

MDPI and ACS Style

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top