Affinity of polyphenols for lipid bilayers

Nakayama, Tsutomu; Hashimoto, Toshihiko; Kajiya, Katsuko; Kumazawa, Shigenori

doi:10.1002/biof.5520130124

Cited by 65 publications

(58 citation statements)

References 12 publications

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“…ECG was previously reported to be more potent to act on liposomal membranes than EGCG. 8,19) In this study, however, the relative membrane activity was reversed between ECG and EGCG. This discrepancy is attributable to the compositional difference of membrane lipids, that is, previous liposomes were prepared with phosphatidylcholine alone, whereas the present ones with different unsaturated phospholipids and cholesterol to resemble tumor cell membranes.…”

Section: Fig 2 Effects Of Egcg On Different Regions Of Cell Membranescontrasting

confidence: 59%

Antiproliferative Effects Associated with Membrane Lipid Interaction of Green Tea Catechins

Tsuchiya

Tanaka

Nagayama

2008

JOURNAL OF HEALTH SCIENCE

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Section: Fig 2 Effects Of Egcg On Different Regions Of Cell Membranescontrasting

confidence: 59%

Antiproliferative Effects Associated with Membrane Lipid Interaction of Green Tea Catechins

Tsuchiya

Tanaka

Nagayama

2008

JOURNAL OF HEALTH SCIENCE

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“…These results and previous findings indicate that the galloyl moiety is responsible for the binding affinity of catechins for HSA. A previous report has shown that the hydrophobicity of the catechins obtained for a 1-octanol/PBS binary liquid was increased drastically by the presence of the galloyl moiety (19). On the other hand, studies of serum albumin-polyphenol interactions suggest that binding of polyphenols with serum albumin are stabilized by hydrophobic interactions, hydrogen-bonding forces, and electrostatic forces (20,21).…”

Section: Discussionmentioning

confidence: 98%

Influence of the Galloyl Moiety in Tea Catechins on Binding Affinity for Human Serum Albumin

Minoda

Ichikawa

Katsumata

et al. 2010

J Nutr Sci Vitaminol

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SummaryThe major catechins of green tea extract are ( Ϫ )-epicatechin (EC), ( Ϫ )-epigallocatechin (EGC), ( Ϫ )-epicatechin gallate (ECg), and ( Ϫ )-epigallocatechin gallate (EGCg). Recent research has indicated that catechins form complexes with human serum albumin (HSA) in blood, and differences in their binding affinity toward HSA are believed to modulate their bioavailability. In this study, we kinetically investigated the interaction between the catechins and HSA immobilized on a quartz-crystal microbalance (QCM). The association constants obtained from the frequency changes of QCM revealed interactions of ECg and EGCg with HSA that are 100 times stronger than those of EC and EGC. Furthermore, comparisons of these catechins by native-gel electrophoresis/blotting with redox-cycling staining revealed that, in a phosphate buffer, ECg and EGCg have a higher binding affinity toward HSA than EC and EGC. These observations indicate that catechins with a galloyl moiety have higher binding affinities toward HSA than catechins lacking a galloyl moiety.

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“…The apparent K m values for EGC glucuronidation by human UGT isozymes and pooled HLM were closer than those for EGCG glucuronidation. This may be due to the much lower binding affinity of EGC than EGCG to microsomal proteins (Wang et al, 1988) and lipids bilayers (Nakayama et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Glucuronides of Tea Catechins: Enzymology of Biosynthesis and Biological Activities

Meng²,

Li³

et al. 2003

Drug Metab Dispos

199

155

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ABSTRACT:(؊)-Epigallocatechin gallate (EGCG) and (؊)-epigallocatechin (EGC) are major green tea catechins with antioxidant and anticancer activities. In this study, we characterized the glucuronidation of EGCG and EGC in human, mouse, and rat microsomes and by nine different human UGT 1A and 2B isozymes expressed in insect cells. Six EGCG and EGC glucuronides were biosynthesized, and their structures were identified for the first time. (؊)-EGCG-4؆-O-glucuronide was the major EGCG glucuronide formed in all incubations. The catalytic efficiency (V max /K m ) for (؊)-EGCG-4؆-O-glucuronide formation followed the order: mouse intestine > mouse liver > human liver > rat liver Ͼ Ͼ rat small intestine. The UGTcatalyzed glucuronidation of EGC was much lower than that of EGCG. The V max /K m for (؊)-EGC-3-O-glucuronide followed the following order: mouse liver > human liver > rat liver > rat and mouse small intestine. Human UGT1A1, 1A8, and 1A9 had high activities with EGCG. UGT1A8, an intestine-specific UGT, had the highest V max /K m for EGCG but low activity with EGC. Mice appeared to be more similar to humans than rats to humans in the glucuronidation of EGCG and EGC. Some of these catechin glucuronides retained the activities of their parent compounds in radical scavenging and in inhibiting the release of arachidonic acid from HT-29 human colon cancer cells. These results provide foundations for understanding the biotransformation and biological activities of tea catechins.

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Affinity of polyphenols for lipid bilayers

Cited by 65 publications

References 12 publications

Antiproliferative Effects Associated with Membrane Lipid Interaction of Green Tea Catechins

Antiproliferative Effects Associated with Membrane Lipid Interaction of Green Tea Catechins

Influence of the Galloyl Moiety in Tea Catechins on Binding Affinity for Human Serum Albumin

Glucuronides of Tea Catechins: Enzymology of Biosynthesis and Biological Activities

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