Interaction of polyphenols with proteins: binding of (-)-epigallocatechin gallate to serum albumin, estimated by induced circular dichroism. Chemical & pharmaceutical bulletin [Chem Pharm Bull (Tokyo)] Journal article | | Title | Interaction of polyphenols with proteins: binding of (-)-epigallocatechin gallate to serum albumin, estimated by induced circular dichroism. | | Author(s) | Nozaki A, Hori M, Kimura T, Ito H, Hatano T | | Institution | Department of Pharmacognosy, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Tsushima, Japan. | | Source | Chem Pharm Bull (Tokyo) 2009 Feb; 57(2):224-8. | | MeSH | Animals
Binding Sites
Catechin
Cattle
Circular Dichroism
Flavonoids
Humans
Indicators and Reagents
Phenols
Protein Binding
Proteins
Serum Albumin
Serum Albumin, Bovine
| | Abstract | The binding of (-)-epigallocatechin gallate (EGCG), a representative natural polyphenol, to human serum albumin (HSA) and bovine serum albumin (BSA) was investigated using induced circular dichroism (CD). The site of the binding EGCG-HSA was analyzed based on the competition with drugs with known binding sites on HSA, such as phenylbutazone (PB) and diazepam (DP). Double-reciprocal plot analyses showed the competitive relations with the site-I- (PB and tolbutamide, TB) and site-II-binding drugs (DP and ibuprofen, IP) indicating the binding of EGCG to sites I and II on HSA, while digitoxin (DG), a site-III-binding drug, did not affect the binding of EGCG. In an analogous way, the competitive relations were observed between EGCG and the site-I- (PB and TB) and site-II-binding (ethacrynic acid, EA) drugs for the binding of EGCG and BSA. The site-III drug DG also showed competitive binding with EGCG to BSA. The binding of EGCG to the albumins indicated its affinity to sites I and II on HSA, while competitive binding for all three sites was observed on BSA. | | Language | eng | | Pub Type(s) | Journal Article
| | PubMed ID | 19182419 |
|
|
| |
Advertise on this site.
| | |
|
