Green Tea Polyphenol Epigallocatechin Gallate Interactions with Copper-Serum Albumin
Epigallocatechin gallate (EGCg), an abundant phytochemical in green tea, is an antioxidant that also binds proteins and complex metals. After gastrointestinal absorption, EGCg binds to serum albumin in the hydrophobic pocket between domains IIA and IIIA and overlaps with the Sudlow I site. Serum alb...
Saved in:
Main Authors: | , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2025-01-01
|
Series: | Molecules |
Subjects: | |
Online Access: | https://www.mdpi.com/1420-3049/30/2/320 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
_version_ | 1832587868218851328 |
---|---|
author | Meiling Fu Liangliang Zhang Rick Killeen Kenneth E. Onugwu Robert M. McCarrick Ann E. Hagerman |
author_facet | Meiling Fu Liangliang Zhang Rick Killeen Kenneth E. Onugwu Robert M. McCarrick Ann E. Hagerman |
author_sort | Meiling Fu |
collection | DOAJ |
description | Epigallocatechin gallate (EGCg), an abundant phytochemical in green tea, is an antioxidant that also binds proteins and complex metals. After gastrointestinal absorption, EGCg binds to serum albumin in the hydrophobic pocket between domains IIA and IIIA and overlaps with the Sudlow I site. Serum albumin also has two metal binding sites, a high-affinity N-terminal site (NTS) site that selectively binds Cu(II), and a low-affinity, less selective multi-metal binding site (MBS). We proposed to determine whether EGCg binds or reacts with Cu(II)-serum albumin using fluorescence, UV–Visible and electron paramagnetic resonance (EPR) spectroscopy. Our results suggest that when serum albumin is loaded with Cu(II) in both sites, EGCg binds to the MBS-Cu(II) and reduces the copper to Cu(I). EGCg does not bind to or react with Cu(II) in the high-affinity NTS site. Potential consequences include changes in copper homeostasis and damage from pro-oxidative Fenton reactions. |
format | Article |
id | doaj-art-995193429bd04e8dac5583de1bcab99a |
institution | Kabale University |
issn | 1420-3049 |
language | English |
publishDate | 2025-01-01 |
publisher | MDPI AG |
record_format | Article |
series | Molecules |
spelling | doaj-art-995193429bd04e8dac5583de1bcab99a2025-01-24T13:43:35ZengMDPI AGMolecules1420-30492025-01-0130232010.3390/molecules30020320Green Tea Polyphenol Epigallocatechin Gallate Interactions with Copper-Serum AlbuminMeiling Fu0Liangliang Zhang1Rick Killeen2Kenneth E. Onugwu3Robert M. McCarrick4Ann E. Hagerman5Department of Chemistry & Biochemistry, Miami University, Oxford, OH 45056, USAInstitute of Advanced Carbon Conversion Technology, Huaqiao University, Xiamen 361021, ChinaDepartment of Anesthesia and Perioperative Medicine, Medical University of South Carolina, Charleston, SC 29425, USADepartment of Chemistry & Biochemistry, Miami University, Oxford, OH 45056, USADepartment of Chemistry & Biochemistry, Miami University, Oxford, OH 45056, USADepartment of Chemistry & Biochemistry, Miami University, Oxford, OH 45056, USAEpigallocatechin gallate (EGCg), an abundant phytochemical in green tea, is an antioxidant that also binds proteins and complex metals. After gastrointestinal absorption, EGCg binds to serum albumin in the hydrophobic pocket between domains IIA and IIIA and overlaps with the Sudlow I site. Serum albumin also has two metal binding sites, a high-affinity N-terminal site (NTS) site that selectively binds Cu(II), and a low-affinity, less selective multi-metal binding site (MBS). We proposed to determine whether EGCg binds or reacts with Cu(II)-serum albumin using fluorescence, UV–Visible and electron paramagnetic resonance (EPR) spectroscopy. Our results suggest that when serum albumin is loaded with Cu(II) in both sites, EGCg binds to the MBS-Cu(II) and reduces the copper to Cu(I). EGCg does not bind to or react with Cu(II) in the high-affinity NTS site. Potential consequences include changes in copper homeostasis and damage from pro-oxidative Fenton reactions.https://www.mdpi.com/1420-3049/30/2/320polyphenolmetalloproteinantioxidantserum albumincoppergreen tea |
spellingShingle | Meiling Fu Liangliang Zhang Rick Killeen Kenneth E. Onugwu Robert M. McCarrick Ann E. Hagerman Green Tea Polyphenol Epigallocatechin Gallate Interactions with Copper-Serum Albumin Molecules polyphenol metalloprotein antioxidant serum albumin copper green tea |
title | Green Tea Polyphenol Epigallocatechin Gallate Interactions with Copper-Serum Albumin |
title_full | Green Tea Polyphenol Epigallocatechin Gallate Interactions with Copper-Serum Albumin |
title_fullStr | Green Tea Polyphenol Epigallocatechin Gallate Interactions with Copper-Serum Albumin |
title_full_unstemmed | Green Tea Polyphenol Epigallocatechin Gallate Interactions with Copper-Serum Albumin |
title_short | Green Tea Polyphenol Epigallocatechin Gallate Interactions with Copper-Serum Albumin |
title_sort | green tea polyphenol epigallocatechin gallate interactions with copper serum albumin |
topic | polyphenol metalloprotein antioxidant serum albumin copper green tea |
url | https://www.mdpi.com/1420-3049/30/2/320 |
work_keys_str_mv | AT meilingfu greenteapolyphenolepigallocatechingallateinteractionswithcopperserumalbumin AT liangliangzhang greenteapolyphenolepigallocatechingallateinteractionswithcopperserumalbumin AT rickkilleen greenteapolyphenolepigallocatechingallateinteractionswithcopperserumalbumin AT kennetheonugwu greenteapolyphenolepigallocatechingallateinteractionswithcopperserumalbumin AT robertmmccarrick greenteapolyphenolepigallocatechingallateinteractionswithcopperserumalbumin AT annehagerman greenteapolyphenolepigallocatechingallateinteractionswithcopperserumalbumin |