A1 Refereed original research article in a scientific journal
Ellagitannins with Glucopyranose Cores Have Higher Affinities to Proteins than Acyclic Ellagitannins by Isothermal Titration Calorimetry
Authors: Karonen M., Oraviita M., Mueller-Harvey I., Salminen J.-P., Green R.J.
Publisher: AMER CHEMICAL SOC
Publication year: 2019
Journal: Journal of Agricultural and Food Chemistry
Journal name in source: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Journal acronym: J AGR FOOD CHEM
Volume: 67
Issue: 46
First page : 12730
Last page: 12740
Number of pages: 11
ISSN: 0021-8561
eISSN: 1520-5118
DOI: https://doi.org/10.1021/acs.jafc.9b04353
Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/44063384
The thermodynamics of the interactions of different ellagitannins with two proteins, namely, bovine serum albumin (BSA) and gelatin, were studied by isothermal titration calorimetry. Twelve individual ellagitannins, including different monomers, dimers, and a trimer, were used. The studies showed that several structural features affected the interaction between the ellagitannin and the protein. The interactions of ellagitannins with proteins were stronger with gelatin than with BSA. The ellagitannin-gelatin interactions contained both the primary stronger and the secondary weaker binding sites. The ellagitannin-BSA interactions showed very weak secondary interactions. The ellagitannins with glucopyranose cores had stronger interaction than C-glycosidic ellagitannins with both proteins. In addition, the observed enthalpy change increased as the degree of oligomerization increased. The stronger interactions were also observed with free galloyl groups in the ellagitannin structure and with higher molecular flexibility. Other smaller structural features did not show any overall trend.
Downloadable publication This is an electronic reprint of the original article. |  | |
Downloadable publication This is an electronic reprint of the original article. | |
