Gillian T. Rich
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Gillian T. Rich has a total of 4 co-authors. Here are the top co-authors by number of shared publications:
- Maria Buchweitz
Department of Food Chemistry, Institute of Biochemistry and Technical Biochemistry, University of Stuttgart, Allmandring 5b, 70569 Stuttgart, Germany
2 shared publications - Paul Anthony Kroon
Quadram Institute Bioscience, Norwich Research Park, Norwich NR4 7UQ, UK
2 shared publications - Peter James Wilde
Quadram Institute Bioscience, UK
2 shared publications - Mark S. Winterbone
Quadram Institute Bioscience, Norwich Research Park, Norwich, UK
1 shared publication
Latest Publications
- Open Access
Towards an Understanding of the Low Bioavailability of Quercetin: A Study of Its Interaction with Intestinal Lipids
We have studied the uptake of quercetin aglycone into CaCo-2/TC7 cells in the presence and absence of mixed micelles that are present in the human small intestine. The micelles inhibited the transport of quercetin into the cells. To gain an understanding of why this is the case we examined the solubilisation of quercetin in micelles of differing composition and into pure lipid phases. We did this by using the environmental sensitivity of quercetin’s UV-visible absorption spectra and measurement of free quercetin by filtration of the micellar solutions. The nature of the micelles was also studied by pyrene fluorescence. We found that the partitioning of quercetin into simple bile salt micelles was low and for mixed micelles was inhibited by increasing the bile salt concentration. The affinity of quercetin decreased in the order egg phosphatidylcholine (PC) = lysoPC > mixed micelles > bile salts. These results, together with the innate properties of quercetin, contribute to an understanding of the low bioavailability of quercetin.
Open AccessTowards an Understanding of the Low Bioavailability of Quercetin: A Study of Its Interaction with Intestinal Lipids
We have studied the uptake of quercetin aglycone into CaCo-2/TC7 cells in the presence and absence of mixed micelles that are present in the human small intestine. The micelles inhibited the transport of quercetin into the cells. To gain an understanding of why this is the case we examined the solubilisation of quercetin in micelles of differing composition and into pure lipid phases. We did this by using the environmental sensitivity of quercetin’s UV-visible absorption spectra and measurement of free quercetin by filtration of the micellar solutions. The nature of the micelles was also studied by pyrene fluorescence. We found that the partitioning of quercetin into simple bile salt micelles was low and for mixed micelles was inhibited by increasing the bile salt concentration. The affinity of quercetin decreased in the order egg phosphatidylcholine (PC) = lysoPC > mixed micelles > bile salts. These results, together with the innate properties of quercetin, contribute to an understanding of the low bioavailability of quercetin.
- Open Access
- 1 November 2016
- Published by Elsevier in Food Chemistry
- Vol. 211, 356-364
Quercetin solubilisation in bile salts: A comparison with sodium dodecyl sulphate
- 1 November 2016
- Published by Elsevier in Food Chemistry
- Vol. 211, 356-364
Open AccessQuercetin solubilisation in bile salts: A comparison with sodium dodecyl sulphate